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Home / Opinion / Online Views / Death of the telegram
Death of the telegram
5 min read . Updated: 15 Jul 2013, 09:21 AM IST Anil Padmanabhan
The increased transport connectivity, first between cities and then between cities and villages on the one hand and the cellphone revolution on the other, rapidly diminished the importance of the telegram. Photo: Mint
(Mint)
The telegram defines the trend that is changing the way communication is reordering our lives
In less than 24 hours, the telegram will cease to exist. The service, which started in India 163 years ago from Kolkata, will, like the steam engine, become a footnote of history from Tuesday. In no uncertain terms, it marks the end of an era.
I am sure the telegram has touched most of us in some form or the other. It would undoubtedly bring forth feelings of nostalgia. But it is much more than that. It defines the trend that is changing the way communication is reordering our lives. Ever since I came across Frances Cairncross's compelling work, The Death of Distance: How the Communications Revolution Is Changing our Lives, I have wondered and marvelled at how our lives have transformed (and continue to transform), even in a country like India, which is still so digitally challenged. The death of the telegram is just another chapter.
My first memory of a telegram, presumably because my parents were migrants in Delhi, was the news about a death, grave illness or birth of someone in our extended family. And, more often than not, the postman's (not the regular mail delivery guy) knock would come after midnight. It is like a late night telephone call can only be, in most instances, the harbinger of bad news.
The telegram itself was a strip of at best two-three strips of paper clumsily stuck on a sheet of paper that was folded to look like an envelope. The message was typed out, often with some very obvious typos, especially when it came to spelling out names. Brevity was the key as each word would cost, unlike say the inland letter, that my parents sent out dutifully every week, which cost some five or ten paisa. In fact, till such time (less than 10 years ago) the telephone directory for the landline used to carry a list of standard telegram messages as suggestions for consumers.
The telegram was a colonial legacy. The first telegraph line in India was laid by the East India Company in 1850 to connect Kolkata and Diamond Harbour, a distance of 43.5km. If history has it right, seven years later it served as a life saver for the British troops who were completely blindsided in the first round of revolt—the 1857 mutiny—by Indian soldiers. But for a telegram, which reached in time for the British to rush fresh troops to the various flashpoints and successfully crush the rebellion, the history of India would have read very differently. (More fascinating details can be gleaned from my colleague Sidin Vadukut's piece here)
After Independence, it worked best in an era when distances were not easily overcome. The increased transport connectivity, first between cities and then between cities and villages on the one hand and the cellphone revolution on the other, rapidly diminished the importance of the telegram. It is exactly what Cairncross had forecast in her book, first published in 1997—distance would cease to be a relevant factor in the conduct of business and personal lives as new communication technologies take root with clicks replacing the bricks economy.
The telegram is just one among the many casualties in this evolution. Online transactions mean that we no longer queue up in a bank to draw or deposit money. We can purchase consumer goods without wading through a market or book airline and train tickets without taking a half-day from work—all instances of the process of disintermediation.
Yes, it is the end of an era and we are entitled to our share of nostalgia. But it also reaffirms the era that began a while ago. Thanks to Aadhaar, India's ambitious programme to arm every resident with a unique identity number, now even identity will become portable. So far, it was rooted in your so-called permanent address, making normal life almost impossible for migrants—rich and poor. Brace for fresh transformation of our lives.
And, yes, if you still feel nostalgic about the telegram, you have two options:
One, log onto http://www.telegramstop.com/ and send out a classic telegram lookalike to anyone, anywhere in the world for a charge of $7.15. Second, open a twitter account and tweet out a message 140 characters long for free.
So, is the telegram really dead or assuming a new avatar?
Anil Padmanabhan is deputy managing editor of Mint and writes every week on the intersection of politics and economics. Comments are welcome at capitalcalculus@livemint.com
India through the years in telegrams
1859: A telegram regarding the movement of rebels in the Bhagalpore area during the revolt of 1857, Photographs courtesy National Archives, Nehru Memorial Library
1864: A telegram regarding police action against the Thugee cult.
1897: Congratulatory telegrams describing felicitations from rulers of princely states to Queen Victoria on the 60th anniversary of her reign (June-July 1897).
1930: A telegram on protests by Indians in Persia in connection with Mahatma Gandhi's arrest in 1930.
1932: Detailed exchanges via telegrams between Gandhi and the government on negotiations leading up to the crucial Second Round Table Conference in London in 1932.
1937-39: Telegrams involving Nehru and Gandhi, with the latter bemoaning corruption in the Congress party in one of these.
1940: Translation of a World War II telegram addressed by the Japanese consul general in India to the Japanese consul in Rangoon, Burma, after a British warship held up the ship Asama Maru and removed Germans on board.
1940: Weekly telegrams from British Indian provinces detailing events during the freedom movement.
1942: Telegrams exchanged between Sir Stafford Cripps and the Viceroy.
1943: Defence department telegrams regarding the escape to Switzerland of Indian prisoners of war during World War II.
1943: Telegrams calling for the release of Gandhi during his fast in February 1943 at the height of the Quit India Movement.
1941-45: Telegrams describing the allegiance of Muslim traders to the Muslim League and the need for such an organization.
1948: Telegrams describing the situation of Indians in Singapore and Malaya.
Telegrams detailing the proposal to summon a special session of the United Nations Security Council for consideration of the Palestine question. These telegrams give a glimpse into India's stance on the issue.
1951-53: Detailed exchanges between the prime ministers of India and Pakistan addressing Kashmir and other issues.
A condolence telegram to Lalita Devi Shashtri on the death of her husband Lal Bahadur Shastri, prime minister of India.
Buy or sell: Vaishali Parekh recommends 3 stoc...


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ON24 Announces Next-Generation Virtual Environment Manager
New Solution Provides Greater Ease of Use, Flexibility for Virtual Environment Producers, Partners and Content Creators
SAN FRANCISCO, Nov. 12, 2013 /PRNewswire/ -- ON24, the global leader in webcasting and virtual communication solutions, today announced the release of the next-generation Virtual Environment Manager (VEM), a new HTML-enabled back-end application for managing virtual environments such as new-hire onboarding and user conferences.
(Photo: http://photos.prnewswire.com/prnh/20131112/SF15054)
(Logo: http://photos.prnewswire.com/prnh/20131016/SF98451LOGO-b)
ON24's next-generation Virtual Environment Manager increases virtual environment ease of use and flexibility. (PRNewsFoto/ON24) (PRNewsFoto/ON24)
"The launch of a new, easy-to-use virtual environment management tool is part of the larger self-service trend we are seeing in our industry," explained Jayesh Sahasi, ON24 Chief Product Officer and CTO. "With the Virtual Environment Manager, producers can easily adapt their virtual communications solutions to meet corporate needs, with easy customization for a variety of applications ranging from leadership training to product launches."
The new VEM offers numerous benefits, including:
Significantly enhanced ease of use via a new user interface and single sign-on to access all ON24's applications
Tighter integration with ON24's webcasting tools
Enhanced permissioning with role-based access
New content management system providing unlimited bulk content uploading and multiple content filtering and sorting options
A new and improved help system
Setting up and managing a virtual environment is now simpler and more intuitive than ever with the new Virtual Environment Manager. For example, a WYSIWYG (What You See Is What You Get) visual editor facilitates creation and management of all locations within the environment. Navigation options are easily configured, added or moved, and the visual editor allows the producer to immediately view changes in real time.
With single sign-on functionality, VEM is a one-stop media content management system that provides integration across ON24 virtual environments and webcasting, enabling webcast access from the virtual environment; for example, users can create, publish and manage webcasts directly within the virtual environment. "VEM delivers a fully integrated and streamlined workflow, saving producers valuable time and resulting in a better end user experience," explained Sahasi.
"One of the most exciting aspects of Virtual Environment Manager is the content management capability," Sahasi added. With VEM, content can be tagged and organized, with role-based access to that content. VEM provides:
Enhanced filtering
Searching capabilities
Bulk uploading
"The new features and functionality in Virtual Environment Manager are a direct result of listening to our customer base and responding to their needs," commented Sahasi. "We are committed to bringing the best experience to everyone involved in producing and consuming virtual communications – the producers, content creators, sponsors and, ultimately, their audiences."
About ON24, Inc.
ON24, the virtual communications platform for the global enterprise, provides interactive, impactful cloud-based solutions that drive outstanding results. ON24 offers a broad and innovative product portfolio, including webcasting, virtual events and virtual environments, accessible from any device and supported by robust reporting and analytics. Applications for the ON24 platform include demand generation, partner enablement, virtual talent onboarding and development, product launches, company town hall meetings and user conferences. More than 800 organizations, including IBM, CA Technologies, Merck, Unilever, JPMorgan Chase, Deloitte, Credit Suisse, Ernst & Young, Amazon and SAP, rely on ON24. The company is headquartered in San Francisco, with offices throughout the world. For more information, visit http://www.ON24.com.
SOURCE ON24

redpajama_set_name: RedPajamaCommonCrawl


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"Midnight at the Bright Ideas Bookstore"
Matthew Sullivan received his B.A. from the University of San Francisco, his M.F.A. from the University of Idaho, and has been a resident writer at Yaddo, Centrum, and the Vermont Studio Center. His writing has been nominated for the Pushcart Prize and other awards, and has won the Florida Review Editor's Prize and the Robert Olen Butler Fiction Prize. In addition to working for years at Tattered Cover Book Store in Denver and at Brookline Booksmith in Boston, he has taught writing and literature at colleges in Boston, Idaho, and Poland, and currently teaches writing, literature, and film at Big Bend Community College in the high desert of Washington State.
Sullivan applied the Page 69 Test to his new novel, Midnight at the Bright Ideas Bookstore, and reported the following:
I love that this scene from page 69 dives right into one of the main threads of the novel! In it, Lydia and David—the protagonist and her beau—are discussing the crate of books that Lydia inherited after one of her customers, a troubled young BookFrog named Joey, committed suicide in the bookstore where she works:
In her kitchen, Lydia nibbled the crust from her honey toast and waited impatiently for her overworked coffeemaker to finish gurgling. When she looked up, David was there in his towel, red from his shower, smelling of menthol shaving cream. He peered into Joey's milk crate, which sat in the center of their breakfast table, where Lydia had left it the night before.
"More books?" he said, picking up Joey's dusty Victorian story primer and turning it over in his hands.
"Can't ever have too many," she said lightly.
"Seriously. I like your whole book thing. Just having them around makes me feel smarter."
"Now, if we could just get you to read them."
"No need. It's like free IQ points in every room. On every conceivable surface."
"Glad to help."
"Some would call you a hoarder," he said. "But not me. I call you a collector."
"That's the spirit," she said.
Lydia looked up the length of David's arm and saw his clean, damp hair and the remnant glow of his shower, and felt the desire to rest her hand on his.
Lydia and David are meant to have a loving banter and a good chemistry as a couple. But as we see here, for all of his kindness, David doesn't share or particularly understand Lydia's bibliophilia.
Throughout much of this novel, I was attempting to raise a glass to books and book lovers, but also to use this particular passion as a glimpse into Lydia's psyche. Beyond acting as her escape, books also act as reminders of her childhood, especially of the happiness she experienced with her librarian father in the years before The Hammerman murders derailed the trajectory of their life. Her early childhood acts as a perpetual Eden to which she is always trying to return. The Bright Ideas Bookstore is as close as she comes to finding that sanctuary again.
Spoiler alert: At the very end of the novel, Lydia ends up feeling more connected to her old friend Raj than to her boyfriend, David… something that has caused some discussion among readers ("Team David or Team Raj?"). The rationale here is that Raj was part of that bookish childhood bliss Lydia has spent her adult life trying to recapture, so he, inevitably, would be the guy who makes her happiest—and who she ends up with. In many ways, David may be a better fit for her, and Raj may be part of an unhealthy nostalgia, but to me there is an emotional truth in Lydia and Raj, in the end, arriving at some approximation of their peaceful life before The Hammerman.
Visit Matthew Sullivan's website.
"Cold Spectrum"
"Devils Within"
"The Rift Frequency"
"The Texan Duke"
"Nightblade's Vengeance"
"Murders.com"
"Forbidden Suns"
"Ghost in the Tamarind"
"The Midnight Dance"
"The Prague Sonata"
"Gray Wolf Island"
"Death on Tap"
"Mr. Rochester"
"The Dark Lake"
"A Hive of Homicides"
"A Beautiful Poison"


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The GOP's Fall Jobs Agenda: Roll Back Regulations and Taxes
By Billy House
In a memo to Republicans, Majority Leader Eric Cantor previewed a slate of bills the House could take up when Congress returns next week
While the spotlight will be on the workings of the new deficit-reduction "super committee" after Congress returns next week, House Republican leaders said on Monday they also have set a legislative agenda for fall and winter that concentrates heavily on regulatory and tax relief.
"When we return next week, the Joint Select Committee on Deficit Reduction will begin meeting to take an additional incremental step toward addressing our debt crisis. During this time, it is essential that the House continue our focus on the jobs crisis," Majority Leader Eric Cantor (R-Va.) said in a memo being sent on Monday to rank-and-file House Republicans.
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In partisan language, Cantor's memo goes on to describe a schedule that includes tackling what he identifies as "10 job-destroying regulations," with more than one of these efforts being intended to highlight legislation from freshmen GOP House members.
In broadest terms, Republicans appear determined to counter Democratic claims that they are not doing enough on the jobs front. Cantor wrote that the various regulations or rules to be targeted "are reflective of the types of costly bureaucratic handcuffs that Washington has imposed upon businesspeople who want to create jobs."
Many of the planned moves are certain to prompt resistance from the Obama administration and Senate Democrats. The office of House Minority Leader Nancy Pelosi (D-Calif.) was expected to release a response to the memo later on Monday.
Cantor wrote that Republicans will kick off their efforts the week of September 12 by seeking to overrule a National Labor Relations Board ruling that restricts Boeing's efforts to move an assembly line from unionized Washington state to South Carolina, a right-to-work state. Business leaders accuse the Obama administration of seeking to to help labor allies. Cantor noted that freshman Rep. Tim Scott (R-S.C.) has introduced legislation to prevent NLRB from "restricting where an employer can create jobs in the United States."
Other regulatory proposals or rules to be targeted in following weeks and months touch on Environmental Protection Agency standards for cross-state air pollution from power plants, boilers, coal ash in mining-heavy states, cement production, and farm dust; new ozone standards; greenhouse-gas performance standards; and some rules under the new health care law.
Cantor also wrote that in the winter, the House will consider legislation in light of an NLRB notice of a proposed rule regarding union election procedures - legislation he said will "protect the interests of both employers and their workers."
On taxes -- another area described as hindering the creation of "middle-class jobs" -- Cantor's memo said House Ways and Means Chairman Dave Camp (R-Mich.) will lead efforts to provide relief for businesses.
Cantor writes that those will include a planned vote on terminating a requirement due to start in 2013 that would mandate federal, state, and local governments to withhold 3 percent of all government payments made to contractors in excess of $100 million. According to Cantor, this move will "lift the uncertainty" being brought upon construction contractors, medical providers, manufacturers, farmers, and many others who provide goods and services under government contracts.
Cantor wrote that Republicans also intend to continue pushing a plan to allow businesses with fewer than 500 employees to take a tax deduction equal to 20 percent of their income. He noted that the goal of the proposal - part of the GOP's 2010 election "Pledge to America," was simple: to "immediately free up funds for small businesspeople to retain and hire new employees, and reinvest in and grow their businesses."
House leaders also expect Obama to advance three free-trade agreements sometime this fall, and Cantor wrote that "when he finally sends them our way, I will not hesitate to schedule them." The protracted battle over the debt limit stalled plans in July to ratify pending trade deals with Colombia, Panama, and South Korea.
Image credit: Jonathan Ernst/Reuters


What a great meeting by great organizers for great people. The ISBS of 1999 in Perth Australia presented the highest scientific quality presented by leaders from all over the World.
Thanks to Dr. Ross Sanders and Dr. Barry Gibson for having such a great organization and great time in superb city of Perth.
This ISBS web page was created by Gideon Ariel (Gideon Crocodile Dundee...), main sponsor of the ISBS-99 meeting. I will try to present the various events we experienced in Perth in the following gallery. In addition, I published step by step instructions, how to download the APAS system from the net and install it on any Pentium based PC, Windows-98 or Windows NT, and how to install the system from the CD which you obtained at the conference.
Again, thank you Ross Sanders and Barry Gibson for providing a great time to all.
The International Society of Biomechanics is Sports (ISBS) is pleased to present the Scientific Proceedings of the XVII International Symposium on Biomechanics in Sports, held at Underwater World, Sorrento Quay, Perth, Western Australia from June 30 to July 6, 1999.
The editors wish to thank the authors for their efforts to comply with the standards required for publication in the Scientific Proceedings of the ISBS. We also thank the members of the Scientific Committee for their competent and thorough reviews.
The International Society of Biomechanics; in Sports is confident that this and future publications will contribute to the major goal of the Society, that is, to 'bridge the gap between sports biomechanics researchers and practitioners in teaching, coaching, training and rehabilitation'. In addition to the scientific program and its proceedings, that goal is also being achieved through 'special activities' and workshops. These include the ongoing work of the ISBS Working Party for Research currently led by Professor Larry Noble. In conjunction with this Symposium a 'workshop on data smoothing' has been conducted by Professor Graeme Wood as a collaborative venture of the International Society of Biomechanics; in Sports and the International Society of Biomechanics. Congratulations to Professor Renato Rodano and Professor Gunter Rau for facilitating this healthy affiliation between the ISBS and ISB. Also, in an attempt to serve coaches and sports people, an'applied program' comprising 26 lectures on topics related to tennis, swimming, fundamental skills, and acrobatics/gymnastics was organised. Notes and proceedings of the foregoing are available through the ISBS.


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package ru.ifmo.kot.track.mvc.model.entity;

/**
 * Created by fanmilan007 on 20.12.2014.
 */

import org.hibernate.annotations.GenericGenerator;

import javax.persistence.*;
import java.sql.Date;

@Entity
@Table(name = "qwikiz")

public class qwikiz {

    @Id
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    @Column(name = "version")
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    @Column(name = "text")
    private String text;

    @Column(name = "date_created")
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    @Column(name = "importance")
    private String importance;

    @Column(name = "complete")
    private String complete;

    @Column(name = "privacy")
    private String privacy;

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        this.text = text;
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        this.importance = importance;
        this.complete = complete;
        this.privacy = privacy;
        this.qedited_user_id = qedited_user_id;
        this.quest_id=quest_id;
    }

    public long getId() {
        return id;
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        this.id = id;
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        return version;
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        this.version = version;
    }

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        return text;
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    public void setText(String text) {
        this.text = text;
    }

    public Date getDate_created() {
        return date_created;
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    public void setDate(Date date_created) {
        this.date_created = date_created;
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    public userz getEdited_user_id() {
        return qedited_user_id;
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        this.qedited_user_id = qedited_user_id;
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    public questz getQuest_id() {
 return quest_id;
 }

 public void setQuest_id(questz quest_id) {
 this.quest_id = quest_id;
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}

redpajama_set_name: RedPajamaGithub


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Catalytic activation of multimeric RNase E and RNase G by 5′-monophosphorylated RNA
Xunqing Jiang and Joel G. Belasco
PNAS June 22, 2004 101 (25) 9211-9216; https://doi.org/10.1073/pnas.0401382101
Xunqing Jiang
Joel G. Belasco
Edited by Stanley N. Cohen, Stanford University School of Medicine, Stanford, CA (received for review February 27, 2004)
Figures & SI
RNase E is an endonuclease that plays a central role in RNA processing and degradation in Escherichia coli. Like its E. coli homolog RNase G, RNase E shows a marked preference for cleaving RNAs that bear a monophosphate, rather than a triphosphate or hydroxyl, at the 5′ end. To investigate the mechanism by which 5′-terminal phosphorylation can influence distant cleavage events, we have developed fluorogenic RNA substrates that allow the activity of RNase E and RNase G to be quantified much more accurately and easily than before. Kinetic analysis of the cleavage of these substrates by RNase E and RNase G has revealed that 5′ monophosphorylation accelerates the reaction not by improving substrate binding, but rather by enhancing the catalytic potency of these ribonucleases. Furthermore, the presence of a 5′ monophosphate can increase the specificity of cleavage site selection within an RNA. Although monomeric forms of RNase E and RNase G can cut RNA, the ability of these enzymes to discriminate between RNA substrates on the basis of their 5′ phosphorylation state requires the formation of protein multimers. Among the molecular mechanisms that could account for these properties are those in which 5′-end binding by one enzyme subunit induces a protein structural change that accelerates RNA cleavage by another subunit.
Messenger RNAs are labile molecules whose longevity directly influences the synthesis rates of the proteins they encode. Despite the importance of mRNA degradation for gene expression, little is understood about the molecular mechanisms that govern differences in mRNA stability, even in so well studied an organism as Escherichia coli. Elucidating these mechanisms is crucial for explaining how RNA sequence and structure control mRNA lifetimes.
The degradation of most E. coli mRNAs is thought to begin with internal cleavage by the endonuclease RNase E (1), although in some cases decay begins instead with cleavage by RNase III or RNase G (an RNase E homolog) (2, 3). The resulting mRNA fragments are then degraded to mononucleotides by a combination of further endonucleolytic cleavage and 3′ exonucleolytic digestion.
RNase E is a 1,061-aa protein comprising functionally distinct domains. The catalytically active amino-terminal half of the protein (N-RNase E: residues 1–498) is alone sufficient for the enzyme's ribonuclease activity, whereas the carboxyl half of the protein (residues 499-1061) contains both an arginine-rich region and a carboxy-terminal domain that serves as a scaffold for the assembly of a multiprotein complex known as the RNA degradosome (4, 5). By contrast, RNase G, which comprises 489 amino acid residues, is similar in sequence to the amino half of RNase E but lacks an arginine-rich region and a scaffold domain (6, 7).
In view of the homology of RNase G to the catalytic domain of RNase E, it is not surprising that they have a similar cleavage site specificity, with both preferring to cut RNA within single-stranded regions that are AU-rich (8, 9). Another important property shared by these two endonucleases is their preference for RNA substrates that bear a single phosphate group at an unpaired 5′ end. Remarkably, such substrates are cleaved by full-length RNase E, N-RNase E, or RNase G more than an order of magnitude faster than otherwise identical RNAs bearing a 5′-terminal triphosphate or hydroxyl group, even though cleavage may occur far from the 5′ end (9–11). The greater susceptibility of 5′-monophosphorylated RNAs to cleavage by these enzymes may help to ensure the rapid degradation of the downstream products of initial endonucleolyic cleavage, which differ from their primary-transcript precursors in being 5′-monophosphorylated rather than 5′-triphosphorylated. Besides helping to minimize the accumulation of downstream mRNA fragments that could serve as templates for the synthesis of aberrant protein products if not promptly destroyed, this property is also likely to contribute to segmental differences in stability within polycistronic transcripts.
Almost nothing is known about the mechanism by which a monophosphate at the 5′ end of an RNA molecule is able to influence the rate of ribonuclease cleavage at an internal site that may be far downstream. Within the catalytic domain of these enzymes, there presumably is a site that can interact productively with RNA 5′ ends that are monophosphorylated but not with those that bear a triphosphate or hydroxyl, yet the presence of such a 5′-end-binding site has not been verified empirically. In principle, the interaction of RNase E or RNase G with the 5′ terminus of a monophosphorylated RNA could accelerate cleavage either by improving the binding affinity of the RNA substrate or by enhancing the catalytic activity of the enzyme. However, even this fundamental question has remained unanswered, in large part because the electrophoretic methods typically used to monitor RNA cleavage by these two ribonucleases have been inadequate for detailed kinetic analysis.
Here we report the design and use of a pair of fluorogenic RNA substrates whose cleavage by RNase E or RNase G can readily be monitored in real time. With these substrates, we have performed detailed kinetic studies of N-RNase E and RNase G. These studies have revealed that the presence of a monophosphate at the 5′ end of an RNA stimulates cleavage by increasing the catalytic efficiency of these enzymes rather than the binding affinity of the RNA substrate and that a 5′ monophosphate can also enhance the specificity of cleavage site selection within an RNA. Additional experiments indicate that each of these ribonucleases must form a homodimer or higher-order multimer for this activation to occur. Together, these findings provide a framework for understanding how the phosphorylation state of the 5′ end is able to influence internal RNA cleavage at distant sites by RNase E and RNase G.
Bacterial Plasmids. Plasmid pNRNE7000, a derivative of pNRNE1000 (11), encodes the first 499 amino acid residues of E. coli RNase E fused at the carboxyl terminus to a hexahistidine affinity tag and a c-Myc epitope tag (GGAAAHHHHHH-VAAEQKLISEEDLNGAARS). Plasmid pRNG1101 encodes E. coli RNase G tagged at the carboxyl terminus with the heptapeptide GHHHHHH (12). Plasmids pMAL-NRNE and pMAL-RNG encode chimeras in which E. coli maltose binding protein has been fused to the amino terminus of E. coli N-RNase E or RNase G, respectively.
Protein Purification. N-RNase E and RNase G bearing a hexahistidine tag were purified from E. coli containing pNRNE7000 or pRNG1101, as described (11). MBP-N-RNase E and MBP-RNase G were purified from lysates of BL21(DE3) containing pMAL-NRNE or pMAL-RNG by affinity chromatography on amylose resin (New England Biolabs). Protein concentrations were determined colorimetrically.
RNA Cleavage Assays. The f luorogenic oligonucleotides P-BR14-FD and HO-BR14-FD were synthesized and HPLC-purified by Xeragon (Huntsville, AL). Internally radiolabeled RNA I.26 bearing a 5′ monophosphate or 5′ triphosphate was synthesized by in vitro transcription with T7 RNA polymerase, as described (11). RNA cleavage was carried out at 25°C in a buffer containing Tris·Cl (25 mM, pH 7.5), MgCl2 (10 mM), NaCl (20 mM), DTT (0.1 mM), and glycerol (5% vol/vol). The cleavage reactions were monitored either continuously by fluorometry with a FluoroMax-2 spectrofluorimeter (excitation at 495 nm; emission at 517 nm) or discontinuously by gel electrophoresis of samples quenched at time intervals with EDTA, followed by analysis with a Molecular Dynamics FluorImager.
Assays of Protein Multimeric State. The subunits of protein multimers were covalently crosslinked in RNA cleavage buffer lacking DTT by treatment with 1,8-bis-maleimidotriethyleneglycol [BM(PEO)3; 3 M, Pierce] for 1 h at room temperature. The protein samples were then dialyzed, concentrated, and analyzed by SDS gel electrophoresis. Protein bands were detected by staining with Coomassie blue or by immunoblot analysis with anti-Myc (Zymed Laboratories) or anti-RNase G (a kind gift from G. A. Mackie) antibodies.
A Fluorogenic Substrate for RNase E and RNase G. To allow RNA cleavage by RNase E and RNase G to be monitored in real time under initial reaction conditions, we developed an oligonucleotide substrate whose digestion by these enzymes results in a marked increase in fluorescence. The sequence of this RNA substrate (BR14-FD; Fig. 1) resembled the 5′-terminal segment of pBR322 RNA I, an untranslated regulatory RNA that contains a single major RNase E cleavage site (13). The key features of the synthetic substrate were a fluorescein tag upstream of the expected RNase E cleavage site and a fluorescence-quenching dabcyl tag downstream of the cleavage site. The bulky fluorescein tag was surrounded by three extra nucleotides to increase its distance from both the 5′ end and the cleavage site. In addition, five of the nucleotides upstream of the cleavage site were 2′-O-methylated to protect them from RNase E digestion (14).
Fluorogenic RNA substrates. Sequence of fluorogenic oligonucleotide substrates in comparison to the segment of RNA I that is cleaved by RNase E. Fluor, fluorescein; Dab, dabcyl. For RNA I, the sequence of only the first nine nucleotides is shown, whereas the three tandem stem-loops that comprise the 3′ portion of RNA I are represented diagrammatically. The principal RNase E cleavage site within the 5′-terminal segment of RNA I is marked with an arrow.
This oligonucleotide substrate, bearing either a 5′-terminal hydroxyl (HO-BR14-FD) or a 5′-terminal monophosphate (P-BR14-FD), was chemically synthesized and purified. Upon complete cleavage by a truncated form of E. coli RNase E (N-RNase E) comprising the catalytic amino-terminal half of the protein (residues 1–499) fused at its carboxyl terminus to an affinity/epitope tag, there was a 30-fold increase in fluorescence at 517 nm due to release of the dabcyl tag, which had quenched most fluorescein fluorescence in the uncleaved RNA (Fig. 8, which is published as supporting information on the PNAS web site).
To confirm that this increase in fluorescence accurately reflected the extent of RNA cleavage, N-RNase E digestion of P-BR14-FD and HO-BR14-FD was monitored by both fluorometry and gel electrophoresis (Fig. 2). As measured by either of these assays, the time course of a cleavage reaction performed under the same reaction conditions was very similar, with the substrate bearing a 5′ phosphate being cleaved 7- to 10-fold faster than the 5′ hydroxyl substrate. As expected, the initial cleavage rates were dependent on the enzyme concentration and saturable at high substrate concentrations (data not shown). Interestingly, whereas N-RNase E cleaved P-BR14-FD at a unique site, its cleavage site specificity was reduced in the absence of the 5′ phosphate. The slow cleavage of HO-BR14-FD to form multiple fluorescent products was Mg2+ dependent and was unaffected by placental ribonuclease inhibitor. Moreover, an N-RNase E variant impaired by mutation of Lys-112 (15) but purified in an identical manner produced the same HO-BR14-FD cleavage products at a diminished rate (data not shown). These findings indicate that the reduction in cleavage site specificity observed for the 5′ hydroxyl substrate is an intrinsic property of N-RNase E.
Fluorometric and electrophoretic assays of enzyme-catalyzed BR14-FD cleavage. (A) Continuous fluorometric assays comparing the cleavage of P-BR14-FD and HO-BR14-FD (1 μM) by N-RNase E (50 nM). (B) Discontinuous electrophoretic assays of P-BR14-FD and HO-BR14-FD cleavage by N-RNase E, performed under the same conditions as in A and analyzed on a 16% polyacrylamide/7 M urea gel. Note the greater cleavage site heterogeneity for the 5′-hydroxyl substrate. Similar results were obtained with RNA substrates lacking 2′-O-methyl groups. The relatively high fluorescence of the uncleaved substrate RNAs in the electrophoretic assay compared to their low fluorescence in solution apparently is caused by spatial separation of the fluorophore and quencher under denaturing conditions, as a similar increase in fluorescence is observed in solution when 7 M urea is present.
Catalytic Activation of RNase E and RNase G by a Substrate Bearing a 5′-Terminal Phosphate. The molecular mechanism by which a 5′-terminal monophosphate can markedly accelerate internal RNA cleavage by RNase E or RNase G is not understood. In principle, this rate acceleration could be a consequence of tighter binding of the 5′-monophosphorylated RNA and/or catalytic activation of the enzyme by this form of the substrate. These two possible explanations can be distinguished by comparing the Michaelis–Menten kinetic parameters k cat and K m for cleavage of substrates bearing a 5′ phosphate versus a 5′ hydroxyl.
To measure k cat and K m for the two fluorogenic substrates, various concentrations of P-BR14-FD or HO-BR14-FD were combined with a limiting amount of N-RNase E, and the initial rate of RNA cleavage was measured by fluorometry. The data were then analyzed on an Eadie–Hofstee plot to allow k cat (y intercept) and K m (slope) to be calculated for each substrate (Fig. 3A ). Whereas k cat was nine times greater for the monophosphorylated substrate (0.83 ± 0.06 min-1) than for the otherwise identical substrate lacking a 5′-phosphate (0.088 ± 0.002 min-1), their K m values were nearly identical (0.60 ± 0.07 μM for P-BR14-FD versus 0.57 ± 0.02 μM for HO-BR14-FD). Similar results were obtained by using E. coli RNase G as a catalyst instead of N-RNase E (Fig. 3B ). In the case of RNase G, the increase in k cat for the monophosphorylated RNA (2.1 ± 0.1 min-1) versus the hydroxyl RNA (0.096 ± 0.010 min-1) was somewhat larger (22-fold), but once again the K m values for the two substrates were similar (0.23 ± 0.03 μM for P-BR14-FD versus 0.33 ± 0.05 μM for HO-BR14-FD). These findings indicate that the presence of a monophosphate at the 5′ end of RNA accelerates its cleavage by RNase E or RNase G by catalytically activating these enzymes rather than by increasing the binding affinity of the RNA substrate.
Comparison of the Michaelis–Menten parameters for ribonucleolytic cleavage of substrates bearing a 5′ monophosphate versus a 5′ hydroxyl. Cleavage of P-BR14-FD and HO-BR14-FD by N-RNase E (75 nM) (A) or RNase G (20 nM) (B) was monitored continuously by fluorometry, and the initial reaction rates measured at various substrate concentrations (0.08–1.20 μM for N-RNase E and 0.05–0.50 μM for RNase G) were graphed as Eadie–Hofstee plots (v, reaction rate; [S], substrate concentration; [E], enzyme concentration). The y intercept of such plots equals k cat, and the slope equals -K m.Inthe two upper graphs, the data for both P-BR14-FD (triangles) and HO-BR14-FD (circles) are shown, whereas in the two lower graphs, the HO-BR14-FD data for N-RNase E (A) and RNase G (B) are replotted in a magnified view in which the scale of both axes has been reduced by a factor of 10.
Importance of Enzyme Multimeric State for Activation. In the course of performing these rate measurements, we discovered that the degree to which a 5′-monophosphate facilitates cleavage by N-RNase E depends on the enzyme concentration. When assayed at a fluorogenic substrate concentration of 0.3 μM, the rate enhancement increased from 2-fold at an N-RNase E concentration of 2.5 nM to 18-fold at an N-RNase E concentration of 100 nM (Fig. 4A ). Near the low end of this enzyme concentration range (5 nM N-RNase E), there was little difference in k cat and almost no difference in K m between the monophosphorylated substrate (k cat = 0.41 ± 0.02 min-1; K m = 0.50 ± 0.05 μM) and the hydroxyl substrate (k cat = 0.18 ± 0.02 min-1; K m = 0.39 ± 0.08 μM) (data not shown), whereas near the high end of the range (75 nM N-RNase E), k cat was much greater for the monophosphorylated substrate than for the hydroxyl substrate (0.83 ± 0.06 min-1 versus 0.088 ± 0.002 min-1; see above). By contrast, no significant concentration dependence was observed for RNase G, which cleaved P-BR14-FD 20–30 fold faster than HO-BR14-FD over a broad range of enzyme concentrations (Fig. 4B ). The influence of N-RNase E concentration on catalytic activation by a 5′-monophosphate was independent of substrate length, as judged from an experiment in which the cleavage rates of a 130- to 185-nt radiolabeled RNA substrate (RNA I.26; ref. 11) bearing either a monophosphate or a triphosphate at the 5′ end were compared at two different N-RNase E concentrations (5 nM versus 75 nM) by an assay involving gel electrophoresis and autoradiography (Fig. 9, which is published as supporting information on the PNAS web site). Once again, the rate enhancement observed for the monophosphorylated substrate was greater at the higher enzyme concentration.
Influence of enzyme concentration on the 5′-end dependence of N-RNase E and RNase G. The ratio of the cleavage rates of P-BR14-FD versus HO-BR14-FD (0.3 μM) is plotted as a function of N-RNase E (A) or RNase G (B) concentration.
The influence of protein concentration on the 5′-end dependence of N-RNase E suggested that the ability of a 5′-monophosphate to catalytically activate this ribonuclease might depend on the enzyme's multimeric state. Of relevance to this hypothesis are recent studies showing that RNase G exists primarily as a homodimer at moderate protein concentrations (16) and that N-RNase E exists primarily as a homotetramer at very high protein concentrations (17). That N-RNase E at lower concentrations can exist as a mixture of protein forms in different multimeric states was indicated by the results of gel electrophoresis under nondenaturing conditions, which revealed both monomeric and dimeric forms of the protein (Fig. 10, which is published as supporting information on the PNAS web site).
To corroborate the latter finding and extend it to a wide range of protein concentrations, we devised an assay of N-RNase E and RNase G multimeric state that involved chemical crosslinking followed by SDS/gel electrophoresis and immunoblotting. N-RNase E at various concentrations was treated with the bifunctional cysteine-crosslinking reagent BM(PEO)3 to covalently join molecules that had formed multimers, and the crosslinked and uncrosslinked forms of the protein were resolved by electrophoresis under denaturing conditions (Fig. 5A ). Quantitative comparison of the relative abundance of the different protein forms revealed a marked concentration dependence (Fig. 5C ). At low concentrations, N-RNase E appeared to be almost entirely monomeric, whereas at higher concentrations a substantial fraction of the protein formed crosslinkable dimers and higher-order multimers. The concentration dependence of multimerization mirrored the effect of protein concentration on the degree to which N-RNase E could be activated by a 5′-monophosphorylated substrate (Fig. 5E ). These results suggest that multimer formation by this enzyme is necessary for its catalytic activation by 5′-monophosphorylated RNA substrates. Depending on the crosslinking efficiency, we calculate that multimeric N-RNase E cleaves the phosphorylated substrate at least 18 times faster than the hydroxyl substrate, whereas monomeric N-RNase E has little, if any, preference for the substrate bearing a 5′-monophosphate.
Correlation of 5′-end dependence and protein multimeric state. (A) Chemical crosslinking of N-RNase E at various protein concentrations. Protein samples (2.5–100 nM subunit concentration) were treated with the bifunctional cysteine crosslinking reagent BM(PEO)3 and then analyzed by SDS/PAGE and immunoblotting. Bands corresponding to monomers (M), crosslinked dimers (D), and crosslinked higher-order multimers (Mult) are marked. The left lane contains a set of protein molecular weight standards. Calibration is in kDa. (B) Chemical crosslinking of RNase G at various protein concentrations. Protein samples (2.5–100 nM subunit concentration) were crosslinked and analyzed by electrophoresis and immunoblotting as in A. (C) Quantitation of the N-RNase E crosslinking data. Traces depicting the relative band intensities in each lane of the immunoblot in A are shown, with vertical scales adjusted to equalize the areas of the monomer peaks. Beside each trace is listed the corresponding protein concentration and the percentage of protein subunits that became crosslinked at that concentration (dimers and higher-order multimers). Arrows identify peaks corresponding to monomer (M) and crosslinked dimer (D) bands. Peaks representing higher-order multimers are to the left of the dimer peak. (D) Quantitation of the RNase G crosslinking data. Vertically adjusted traces depicting the relative band intensities in each lane of the immunoblot in B are shown, along with protein concentrations and the percentage of protein subunits that became crosslinked at each concentration. Only the traces for RNase G concentrations ≥10 nM are shown, because the bands at lower concentrations were too weak to be quantitated. (E) 5′-end-dependent rate acceleration (P-BR14-FD versus HO-BR14-FD, 0.3 μM) as a function of percent crosslinked multimer, as measured at various N-RNase E concentrations (2.5–100 nM).
A similar crosslinking analysis was performed to assess the concentration dependence of RNase G multimerization (Fig. 5B ). The yield of crosslinked RNase G was very high and essentially invariant over a wide range of protein concentrations (Fig. 5D ). Assuming a crosslinking efficiency of 63% for multimeric RNase G under these reaction conditions, the data suggest that, unlike N-RNase E, this protein exists almost entirely as a dimer or higher-order multimer at the concentrations tested. This finding is consistent with recent sedimentation velocity studies (16) and with the lack of a significant effect of enzyme concentration on the marked 5′-end dependence of RNase G within this concentration range (Fig. 4B ).
The importance of multimer formation for the accelerated cleavage of substrates bearing a 5′-monophosphate was confirmed by examining protein chimeras in which E. coli maltose-binding protein (MBP) was fused to the amino terminus of N-RNase E or RNase G. The presence of the MBP domain was found to prevent multimer formation by both of these proteins, as judged by crosslinking with BM(PEO)3 (Fig. 6A ). As a consequence, the ability of N-RNase E and RNase G to cleave 5′-monophosphorylated RNA faster than 5′-hydroxyl RNA was virtually abolished in the context of these MBP chimeras (Fig. 6C ). Moreover, both P-BR14-FD and HO-BR14-FD were cut by MBP-N-RNase E with the reduced cleavage site specificity previously observed only for the 5′-hydroxyl substrate in digests by N-RNase E (Fig. 6B ).
Effect of an amino-terminal maltose-binding protein domain on the dimerization and 5′-end dependence of N-RNase E and RNase G. (A) Chemical crosslinking of N-RNase E, RNase G, MBP-N-RNase E, and MBP-RNase G. Samples of each protein (350 nM) were either treated with the cysteine crosslinking reagent BM(PEO)3 (+) or left untreated (-), and then analyzed by electrophoresis on an SDS/polyacrylamide gel beside a set of protein molecular mass standards (M). Bands for N-RNase E (59.1 kDa), RNase G (56.2 kDa), MBP-N-RNase E (99.3 kDa), and MBP-RNase G (98.4 kDa) were detected by staining with Coomassie blue. (B) Electrophoretic analysis of the cleavage of HO-BR14-FD and P-BR14-FD (0.3 μM) by MBP-N-RNase E (75 nM). (C) Comparative fluorometric analysis of the rate of cleavage of P-BR14-FD and HO-BR14-FD (0.3 μM) by N-RNase E versus MBP-N-RNase E and by RNase G versus MBP-RNase G (75 nM).
For a variety of reasons, traditional electrophoretic techniques for monitoring RNA cleavage by RNase E or RNase G are not adequate for performing the initial rate measurements needed for in-depth kinetic analysis of enzyme function. Moreover, these methods are very slow and laborious. Even an improved analytical method that has recently been described (18) is based on a discontinuous assay in which reaction samples for each time point must be fractionated individually by chromatography.
The fluorogenic RNase E/G substrates that we have developed have a number of significant advantages. These RNAs are commercially available and nonradioactive, and they can be stored for prolonged periods without detriment. No specialized equipment is required to monitor their enzyme-catalyzed cleavage, which results in a marked increase in fluorescence that is readily quantifiable by using an ordinary fluorimeter. This continuous assay method allows initial reaction rates to be measured very quickly (several rate measurements can be completed per hour) and with a high degree of accuracy and sensitivity. Such an approach has been used in studies of RNase A (19, 20).
We have used a matched pair of fluorogenic substrates and either N-RNase E or RNase G to compare the Michaelis–Menten parameters k cat and K m for the cleavage of RNAs that differ only in their 5′ phosphorylation state. Our data show that the presence of a 5′-terminal monophosphate accelerates RNA cleavage by these enzymes not by increasing their RNA-binding affinity, as reflected by K m, but rather by enhancing their catalytic efficiency, as evidenced by a marked increase in k cat.
This finding has important implications for the molecular mechanism of the 5′-end dependence of RNase E and RNase G. Because a monophosphate at the RNA 5′ end is preferred over either a triphosphate, a hydroxyl, or an m7G(5′)ppp(5′)G cap (9–11), which are structurally dissimilar, it seems likely that a 5′-terminal monophosphate can interact physically with these ribonucleases and stimulate RNA cleavage rather than that each of the other 5′-terminal functional groups can interact in an inhibitory manner. Binding of the 5′ monophosphate appears to occur in conjunction with the binding of one or more 5′-terminal nucleotides, because the stimulatory effect of a 5′ monophosphate on RNase E is abolished by 5′-terminal base pairing (10). The free energy associated with the proposed interaction of the monophosphorylated RNA 5′ end with RNase E or RNase G apparently is used not to increase the strength of substrate binding but rather to augment the catalytic power of these enzymes. In principle, enzyme activation by a 5′ monophosphate bound outside the active site could be achieved through a change in protein conformation that improves the orientation and/or catalytic potency of important amino acid residues within the active site. Alternatively, a 5′-terminal monophosphate might be able to participate directly in catalysis by binding inside the active site together with the scissile phosphodiester bond and functioning as a catalytic group in RNA cleavage.
Our finding that the 5′-end dependence of N-RNase E and RNase G correlates with the formation of dimers and higher-order multimers indicates that multimerization is necessary for the catalytic activation of these enzymes by 5′-monophosphorylated RNA substrates. The influence of the enzymes' multimeric state on catalysis suggests specific mechanisms that could account for this property (Fig. 7). For example, if, in addition to a catalytic active site, each multimer subunit has a discrete 5′-end binding pocket that is functionally interconnected exclusively with the active site of another subunit, the occupancy of this 5′-end binding pocket would influence only the catalytic activity of the opposite subunit (trans-activation) and not that of the same subunit. Alternatively, the requirement for multimer formation would be explained if RNase E and RNase G cleave RNA via an alternating sites mechanism in which the active site of one multimer subunit functions as the 5′-end binding pocket that accelerates RNA cleavage by the active site of another subunit. An attractive feature of this model is that enzyme-catalyzed RNA cleavage would generate a new monophosphorylated 5′ end already bound at an active site, potentially facilitating further digestion of the 3′ cleavage product at downstream positions and thereby enhancing the processivity of mRNA decay (21). Finally, unlike the subunits of multimeric RNase E or RNase G, which may become activated when a monophosphorylated RNA 5′ end binds to the same subunit as the scissile phosphodiester bond (cis-activation), isolated monomers of these proteins might fold in a way that precludes their activation, either by inhibiting 5′-end binding or by preventing the bound 5′ end from enhancing catalysis.
Possible mechanisms for the multimerization dependence of 5′ activation of RNase E and RNase G. (Top) Transactivation by 5′-end binding to a distinct site on another subunit. (Middle) Transactivation by 5′-end binding to the active site of another subunit (alternating sites mechanism). (Bottom) Cis-activation by 5′-end binding to a site on the same subunit. In these models, catalytically activated RNase E/G subunits are depicted as round molecules that have a large pair of scissors in the active site, whereas unactivated RNase E/G subunits are drawn as rectangular molecules with a small pair of scissors in the active site. RNAs are represented as curved lines, and 5′-terminal monophosphates are represented as black circles.
Electrophoretic examination of the cleavage products of the fluorogenic oligonucleotides used in these studies indicates that 5′ monophosphorylation can both accelerate cutting at the primary RNA cleavage site and inhibit cleavage at nearby secondary sites. This increase in cleavage site specificity depends on the productive interaction of the RNA 5′ terminus with N-RNase E and can be abolished by an amino-terminal modification of N-RNase E that prevents the enzyme from cutting monophosphorylated RNA at a faster rate. Presumably, this interaction induces significant structural changes in the active site that both enhance catalytic activity and constrain substrate binding so as to restrict the enzyme's choice of cutting sites.
We are grateful to Atilio Deana for helpful comments on the manuscript. These studies were supported by National Institutes of Health Research Grant GM35769.
↵ * To whom correspondence should be addressed. E-mail: belasco{at}saturn.med.nyu.edu.
This paper was submitted directly (Track II) to the PNAS office.
Abbreviation: BM(PEO)3, 1,8-bis-maleimidotriethyleneglycol.
Copyright © 2004, The National Academy of Sciences
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Proceedings of the National Academy of Sciences Jun 2004, 101 (25) 9211-9216; DOI: 10.1073/pnas.0401382101
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Apple has partnered with Vevo to stream its first iTunes Festival in the US.
The concert series kicks off Tuesday night in Austin, TX at the SXSW conference.
Vevo will be streaming concerts of the 15 different artists through apps on iOS and Apple TV. Furthermore, Vevo's website has a page with the stream, but you'll need to be using Safari for it to work.
Like in years past, Apple will also be streaming the iTunes Festival for free via the iTunes Store on iPhone, iPad, iPod touch, Mac or PC, or accessed on demand after. The gigs will also be available to watch through the iTunes Festival app on iOS devices or in HD on Apple TV.
This marks the first iTunes Festival in the US, festivities that have been reserved for London in the past. The SXSW show is a blend of music, film and interactive entertainment from 11 to 16 March, making it a perfect place for the iTunes Festival to debut across the pond.
"We're excited about the incredible line-up of artists performing and SXSW is the perfect place to debut the first iTunes Festival in the US," said Eddy Cue, Apple's senior vice-president of internet software and services.
We've compiled the show times below.


A two-year-old boy had an extensive facial eruption of juvenile xanthogranuloma. The lesions were atypical clinically and histologically and were of 21 months' duration. Although biopsies obtained at the ages of 19 and 20 months suggested a diagnosis of histiocytosis X, his benign course, unremarkable physical examination, and normal findings from laboratory investigations favored a less ominous process. A third skin biopsy showed a dermal infiltrate composed of large, foamy cells and a moderate number of Touton giant cells. On electron microscopy the macrophages contained numerous lysosomes, myelin figures, altered mitochondria, and lipid droplets lacking a limiting membrane consisting with the findings in a previous study of juvenile xanthogranuloma. Langerhans' granules characteristic of histiocytosis X were absent.


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Fervor Coulee
Roots, Toots n' Hoots
Punch Brothers play it precise
State Theatre, Portland, Maine, March 7, 2015
Reviewed by Fred Frawley
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As The Punch Brothers took the stage for their two-song encore, an exuberant fan yelled out, "You're so good, you suck." Banjo player Noam Pikelny repeated the imprecation for the rest of the crowd, and then Punch Brothers' leader Chris Thile did the same. The Punch Brothers are good. They don't suck. But, their craftsmanship and discipline is so precise that improvisation and emotion take a back seat.
The Portland stop was the last on the first leg of Punch Brothers' road tour supporting their new album " Phosphorescent Blues," released in February. "Blues" is strong melodically and technically; the live show showcases many of the selections from the release.
Thile, master mandolinist and vocalist carries a lot of the weight of the live show, which makes sense given his role as ringleader. Since the roughly 90 minutes on stage was devoted to exposing the new material as well as bringing back some Punch Brothers' standards (such as "Ahoy!" and "New York"), the band stayed very close to the songs as recorded. Visual and sound cues were startlingly crisp. In short, the show was a beautiful, energized technical achievement hitting all the marks.
The problem is that each of the Punch Brothers is a masterful musician who, with different performance parameters, can shred. It seems a shame to have Chris Eldredge stand on stage for nearly two hours and know that he could drop the crowd to its knees with some flatpicking at any moment. Pikelny on banjo had some bright licks, especially when in counterpoint with Thile's mandolin. Fiddle player Gabe Witcher excelled, and even contributed some percussive elements when needed. Bassist Paul Kowert shone whenever given the chance.
But, the Punch Brothers is Thile's show, despite the bench strength of his band mates. Thile's mandolin playing seems effortless (it's not). More than one member of the crowd be seen just shaking their head in disbelief as Thile ran off a cross-picking burst out of nowhere, or an impossibly facile run up and down the neck of his instrument. Thile's vocal range starts high and goes higher, an acquired taste.
The last time the Punch Brothers came to these parts, they did well at a smaller venue and graduated to this big room. The Punch Brothers delivered on their value proposition - promoting the new CD. For those looking for a more free-form approach, (and each Punch Brother can deliver vicious improvisational licks), a bluegrass festival setting might hold greater hope.
© Country Standard Time • Jeffrey B. Remz, editor & publisher • countrystandardtime@gmail.com
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Can the Von Duprin 5100 electric strike be used on a pair of doors?
What are the current and voltage requirements of the 10-042 strike?
Why won't the 5100 24v strike work on both a RH & LH door?
Can 5100 electric strikebe used on fire rated door?
Resolution: The Von Duprin 5100 electric strike is not for fire rated applications.
Which electric strike do I use for cylindrical locks used in a single door?


Boy am I sticky! I really shouldn't be, since this is Colorado and it's supposed to be super-dry, but sticky I am. My plan is to convince Drew to go swimming upon his waking up. Wish I had time to go tubing – it seems pretty big out here, what with all of these rivers out here that are really super-wide streams about 3 feet deep. Maybe one of these weekends.
Work is still super busy. Am slowly plowing through Job #2, and Job #1 has gotten a bit easier now that I've more or less figured out how to use a Mac, and how to use Codeigniter, and how to use all of the other stuff they have me using. It's been educational – I'm still not sure how much longer this job will last, but when it ends I'll have some good stuff to spruce up my resume & portfolio with.
On a completely unrelated note, all of the tank tops at Old Navy got stupid. I really like their ribbed tank tops – they're comfortable and usually about $5-$7 each. However, at some point recently they decided to add a foot in length to them. I don't see the point, I wear the shirt and have a giant pile of fabric bunched around my waist? So anyhow, I lost my tank top source, and need to find another one as my tank tops are slowly fraying apart!
Cow appreciation day last weekend was successful, we hit 4 different Chick-fil-as. The best one was in Larkridge, everyone was super excited, there were balloons everywhere and the employees seemed really into the event, and lots of customers were dressed up. We got our picture taken, too. The worst was some CFA in NE Denver (Brighton?), we drove through the middle of nowhere only to find unenthusiastic staff, very few people dressed up, and a few customers that snickered at our costumes. Not appropriate!


text:
Peterborough owes its
prosperity to a monastery
and the modern railways
Peterborough's 17th-century Guildhall was built by John Lovin in 1671 (Photograph: Patrick Comerford, 2019)
I spent much of yesterday [13 August 2019] in the cathedral city of Peterborough. Although I had passed through Peterborough before on train journeys between Cambridge and Birmingham, this was my first time to visit the city and its cathedral.
Peterborough, with a population of about 200,000, was historically part of Northamptonshire, but is now in Cambridgeshire. It is about 110 km east of Birmingham, about 63 km north-west of Cambridge, and 120 km north of London. It stands on the banks of the River Nene which flows into the North Sea about 50 km to the north-east. in some parts of the surrounding countryside, the land lies below sea level, and parts of the Fens are to the east of Peterborough.
There is archaeological evidence of an early Roman presence here. The Romans established a fortified garrison town at Durobrivae on Ermine Street, 8 km to the west in Water Newton, in the mid-1st century AD. There was also a large 1st century Roman fort at Longthorpe, designed to house half a legion, or about 3,000 soldiers, and it may have been set up as early as AD 44-48.
But the city really dates from the Anglo-Saxon period, when a monastery was established at Medeshamstede, which would later become Peterborough. Medeshamstede may have been an Anglian settlement before AD 655, when Sexwulf founded a monastery on land he had been granted to him by Peada of Mercia, who converted to Christianity.
The name of Medeshamstede was changed to Burgh from the late 10th century, possibly after Abbot Kenulf had built a defensive wall around the abbey.
In the Anglo-Saxon resistance to the Norman conquest of England after the Battle of Hastings in 1066, Hereward the Wake rampaged through this town in 1069 or 1070. But the Abbot, Turold, fought back and built a fort or castle outside the deanery garden, now called Tout Hill.
The abbey church was rebuilt and greatly enlarged in the 12th century and the town eventually developed into the Peterborough, although it did not become a borough until the 12th century. The Monastery of Saint Peter, Saint Paul and Saint Andrew was rebuilt in its present form between 1118 and 1238. The burgesses received their first charter from Abbot Robert – probably Robert of Sutton (1262–1273).
With the dissolution of the monastic houses during the reign of Henry VIII, the abbey church became the cathedral at the centre of the new Diocese of Peterborough in 1541, when the last abbot was made the first bishop and the abbot's house became the episcopal palace. The first of Henry's six wives, Katharine of Aragon, was buried in this cathedral when she died in 1536.
Later, Mary Queen of Scots was also buried here after her execution in 1587, but her son, James I, later moved her body to Westminster Abbey, which I visited again on Monday afternoon.
During the English Civil War, Peterborough was divided between the Royalist supporters of King Charles I and the Parliamentarians, and the war reached Peterborough in 1643 when soldiers arrived in the city to attack Royalist strongholds at Stamford and Crowland.
While Peterborough was in the Parliamentarian hands, the Puritan soldiers ransacked the cathedral and destroyed the Lady Chapel, the chapter house, the cloisters, the high altar and the choir stalls, as well as mediaeval decorations, tombs, monuments and records.
The Manor House, Peterborough … the Dean and Chapter of Peterborough succeeded the abbot as lords of the manor (Photograph: Patrick Comerford, 2019)
Peterborough's 17th-century Guildhall, facing the west end of the cathedral, was built in 1671 by John Lovin, who also restored the bishop's palace shortly after the restoration of King Charles II. The Guildhall stands on columns, providing an open ground floor for the butter and poultry markets that were once held there.
The Dean and Chapter of Peterborough Cathedral, who had succeeded the abbot as lords of the manor after the dissolution, retained their own court leet until the municipal borough was incorporated in 1874 with a mayor, six aldermen and 18 councillors.
Peterborough became a modern city with the arrival of the railways in the 19th century, and became an industrial centre known for brick manufacture. The railway enabled large-scale brick-making and distribution to develop, and the area remained Britain's leading producer of bricks for much of the 20th century.
Perkins Engines was established in Peterborough in 1932 by Frank Perkins, creator of the Perkins diesel engine.
The Market Place was renamed Cathedral Square and the adjacent Gates Memorial Fountain moved to Bishop's Road Gardens in 1963, when the then weekly market was moved to the site of the old cattle market.
Peterborough was designated a New Town in 1967, and the city's population grew by almost 50% the two decades between 1971 and 1991. Queensgate shopping centre was opened by Queen Beatrix of the Netherlands in 1982, Thomas Cook and Pearl Assurance moved to Peterborough an urban regeneration company was put in place, with a £1 billion redevelopment of the city centre.
Below the cathedral, Peterscourt on City Road was designed by Sir George Gilbert Scott in 1864, housing Saint Peter's Teacher Training College for men until 1938. The building is mainly listed for the 18th century doorway, which was brought from the Guildhall in London following war damage.
The Diocese of Peterborough covers about 3,100 sq km (1,200 square miles), including the Northamptonshire, Rutland and Peterborough, but parts of the city south of the river, which were once in Huntingdonshire, are in the Diocese of Ely, which includes the rest of Cambridgeshire and much of west Norfolk.
Peterborough Cathedral is one of the most intact large Norman buildings in England and is renowned for its imposing early English Gothic West Front which, with its three enormous arches, is without architectural precedent and with no direct successor.
But more about Peterborough Cathedral later this week, hopefully, and some of the other buildings I visited in Peterborough this week.
The 18th century doorway of Peterscourt was brought from the Guildhall in London following war damage (Photograph: Patrick Comerford, 2019)
Labels: Architecture, Birmingham, Cambridge, Cathedrals, Church History, Local History, Monasticism, Peterborough, Travel
'Patriotism is not enough. I must have no hatred o...
Peterborough owes its prosperity to a monastery an...


Inside Manhattan's Meatpacking district sits the massive, 16,000-square-foot Buddakan, an Asian fusion restaurant, in what used to be a Nabisco cookie factory. Set up like a Chinese mansion, the restaurant boasts a two-story great hall with chandeliers hanging above a 30-person table, and off of that are several small dining rooms with Chinese antiquity painted on the walls. The menu is a mix of traditional Chinese dishes, like the Cantonese spring rolls, and more updated selections, such as the sizzling short rib with mushroom chow fun and glazed black cod.


text:
Financial Advisor / Wealth Manager
New York Life Insurance Company San Antonio, TX
Posted: over a month ago
$50,000 to $300,000 Yearly
Benefits: life_insurance, medical, vision, 401k, dental
Career Description: New York Life financial planners help clients identify and achieve their financial goals. New York Life is dedicated to prudent financial management, high quality products and impeccable service. In addition to superior life and annuity products, registered representatives can offer a comprehensive array of investment products and services to help investors develop a sound, long-term investment strategy. Through NYLIFE Securities registered representatives can provide a variety of competitive products and services, including access to over 12,000 mutual funds, publicly traded stocks, bonds, brokerage CDs, and money market instruments.
Training and Professional Development: New York Life offers a comprehensive three-year paid training program, full marketing support, as well as prospecting and technical assistance. Our mentoring programs give you the opportunity to work with highly successful, established agents and managers who will assist you in developing a clientele. New York Life provides the resources and ongoing support of a Fortune 100 company, with the freedom and autonomy of running your own practice.
You will be in business for yourself - but never by yourself.
Qualifications: We require highly motivated, entrepreneurial individuals who are willing to invest their time and energy into creating profitable and rewarding careers. The candidate we seek must possess uncompromising integrity and the ability to articulate and communicate complex ideas.
Facts about New York Life: New York Life is among the strongest and most respected financial companies in America today. For 61 consecutive years, New York Life has led the Million Dollar Round Table, with more members than any other financial institution in the world. New York Life has the highest possible ratings from each of the four major rating companies: A.M. Best, Standard & Poor's, Moody's, and Fitch. BusinessWeek recognized New York Life as one of the "50 best companies to launch a career". Fortune Magazine recognized New York Life as one of "America's Most Admired Companies".
As a mutual company, we are accountable only to you. That means we are fully aligned with our policy owners, not with outside investors or Wall Street. This allows us to focus on delivering lifelong value to our customers. As a mutual company, with no investors or outside owners, New York Life is uniquely aligned with our clients' interests and priorities. New York Life has been around for 175 years of industry success. We are a Fortune 100 company and are ranked No. 73 on the Fortune 500 list in 2019. New York Life is the Largest Mutual Insurer in the U.S. We have been in business since 1845, and we have a long and impressive track record of helping generations of Americans protect their families and attain their financial goals. That passion and commitment to protection have continued unabated for nearly two centuries. We've seen the nation evolve and events that have affected the lives of Americans: from the Civil War, to the 1906 San Francisco earthquake, to the 1929 stock market crash, to September 11, 2001, to Hurricane Katrina in 2005. What does this mean? It means that New York Life is resilient and able to thrive in all economic conditions. This means we'll always be there for our policy owners, and for future generations.
*Registered Representatives are affiliated with NYLIFE Securities (member FINRA/SIPC), a Licensed Insurance Agency. Financial Advisors are affiliated with Eagle Strategies LLC, a Registered Investment Advisor. NYLIFE Securities and Eagle Strategies are New York Life companies.
1 New York Life has received the highest financial strength ratings currently awarded to any U.S. life insurer by Standard & Poor's (AA+); A.M. Best (A++); Moody's (Aaa); and Fitch (AAA). Source: Individual Third-Party Ratings Reports as of 7/30/18.
2 MDRT (Million Dollar Round Table) is recognized throughout the industry as the standard of excellence in life insurance sales performance. SOURCE: MDRT as of 7/1/2019
3 Based on Fortune Magazine 'Worlds Most Admired Companies' 2019 ranking: https://fortune.com/worlds-most-admired-companies/ To determine the best-regarded companies in 52 industries, Korn Ferry asked executives, directors, and analysts to rate enterprises in their own industry on nine criteria, from investment value and quality of management and products to social responsibility and ability to attract talent. A company's score must rank in the top half of its industry survey to be listed.
4 Based on revenue as reported by "Fortune 500 ranked within Industries, Insurance: Life, Health (Mutual)," Fortune magazine, 6/1/19. For methodology, please see http://fortune.com/fortune500/.
New York Life Insurance Company is an equal opportunity employer M/F/Veteran/Disability/Sexual Orientation/General Identity
SMRU 1822201 11/1/21
New York Life Insurance Company
Great benefits, meaningful impact in the community and amazing culture. Telecommuting options.
As a mutual company, we are accountable only to you. That means we are fully aligned with our policy owners, not with outside investors or Wall Street. This allows us to focus on delivering lifelong value to our customers. As a mutual company, with no investors or outside owners, New York Life is uniquely aligned with our clients' interests and priorities. New York Life has been around for 175 years of industry success. We are a Fortune 100 company and are ranked No. 73 on the Fortune 500 list in 2019. New York Life is the Largest Mutual Insurer in the U.S. We have been in business since 1845, and we have a long and impressive track record of helping generations of Americans protect their families and attain their financial goals. That passion and commitment to protection have continued unabated for nearly two centuries. We've seen the nation evolve and events that have affected the lives of Americans: from the Civil War, to the 1906 San Francisco earthquake, to the 1929 stock market crash, to September 11, 2001, to Hurricane Katrina in 2005. What does this mean? It means that New York Life is resilient and able to thrive in all economic conditions. This means we'll always be there for our policy owners, and for future generations. *Registered Representatives are affiliated with NYLIFE Securities (member FINRA/SIPC), a Licensed Insurance Agency. Financial Advisors are affiliated with Eagle Strategies LLC, a Registered Investment Advisor. NYLIFE Securities and Eagle Strategies are New York Life companies. 1 New York Life has received the highest financial strength ratings currently awarded to any U.S. life insurer by Standard & Poor's (AA+); A.M. Best (A++); Moody's (Aaa); and Fitch (AAA). Source: Individual Third-Party Ratings Reports as of 7/30/18. 2 MDRT (Million Dollar Round Table) is recognized throughout the industry as the standard of excellence in life insurance sales performance. SOURCE: MDRT as of 7/1/2019 3 Based on Fortune Magazine 'Worlds Most Admired Companies' 2019 ranking: https://fortune.com/worlds-most-admired-companies/ To determine the best-regarded companies in 52 industries, Korn Ferry asked executives, directors, and analysts to rate enterprises in their own industry on nine criteria, from investment value and quality of management and products to social responsibility and ability to attract talent. A company's score must rank in the top half of its industry survey to be listed. 4 Based on revenue as reported by "Fortune 500 ranked within Industries, Insurance: Life, Health (Mutual)," Fortune magazine, 6/1/19. For methodology, please see http://fortune.com/fortune500/. New York Life Insurance Company is an equal opportunity employer M/F/Veteran/Disability/Sexual Orientation/General Identity SMRU 1822201 11/1/21
8000 IH 10 West San Antonio
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The witnesses are children of approximately 16 years of age.
The witnesses are children of approximately 16 years of age. When the officers came to my home they did not arrest me but took a photo of my face asked to see my vehicle and my drivers license and asked my occupation, which is , I am a 100% disabled vet and issued me a ticket and left.
I would like to help you, but I need more information. Could you explain the situation more and tell me exactlly what your question is?
On monday I will seek an attorney, being a 100% disabled vet I dont make a whole lot of money, but this situation happened once b4 and i just accepted a no contest, not this time, I'm so angry ...she's not going to get away with it and am thinking of sue for deformation of character slander, liable, and filiong a false police report and lying to a police officer, thinking of a 6 figure suit.
I absolutely doubt that anything will happen. If they thought you had a gun and were a real threat they would have hardly just cite you for a driving ticket and go away. Your ticket can easily be fought and won because of the witnesses and the idea that she lied.
As I said they knew she lied or they would have taken you in and searched your house for a gun.
You had a traumatic experience. Try to remember you will have a lawyer to shoulder some of this stress. Also, come here anytime if you have questions. We're always glad to help! You got into a terrible situation, and it's only been a short time. Give yourself time to calm down. My best to you!!


text:
What Does a B2B Marketing Team Look Like in the Metaverse?
by Robert Henderson
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As an entrepreneur, I often think about how advancements in technology will influence ways companies operate and serve customers.
By now, almost every business founder is thinking about or discussing the metaverse. It's come up in conversation among colleagues, clients, friends, even at home. My focus has been on the impact the metaverse will have on the workplace, B2B marketing, and sales.
B2B marketers have proven to be slow in adopting technologies of the digital age, ultimately paying the price for their tardiness. Rather than repeating history, marketers and salespeople should start to familiarize and immerse themselves in the metaverse now.
At Connect 2021 in October, Mark Zuckerberg introduced a rebranded Facebook as Meta, announcing the company's new mission to bring the metaverse to life.
"Video has become the main way that we experience content...but this isn't the end of the line. The next platform in media will be even more immersive. An embodied Internet where you're in the experience, not just looking at it. We call this the metaverse," Zuckerberg said.
Marketers and salespeople should see the metaverse as a 3D place on the Internet that will completely change the way we consume content and interact with one another. It presents opportunities to reach new customers and audiences more easily while creating unique and personable virtual experiences.
Elements of the metaverse are already being implemented. For gamers who are fans of Roblox, Fortnite, and Second Life, the metaverse has been here for some time. Now, companies in other industries, such as fashion, luxury, and NFTs are investing heavily in the metaverse and other virtual realities to get closer to customers.
It's only a matter of time before workplaces begin participating in all the metaverse has to offer.
How will the metaverse change the way a B2B marketing team functions?
Many people starting out their careers in sales or a trade will say that they learned their skills on the job. For me, too, having that face-to-face, in-person training was crucial to how well I performed my duties and interacted with my teammates.
The pandemic has changed how we work, and although remote, hybrid, and flexible work schedules offer many advantages both to employers and to their staff, there are downsides. What happens when 20% of your workforce isn't geared for in-person work? There's going to be an efficiency challenge.
That's where the metaverse comes in. It can actually be a solution and proxy for working in the office that is more efficient than Zoom, phone, and video.
The metaverse will allow sales teams to provide their staff access to coworkers, calls, and meetings, no matter their location, adding a layer of transparency that is often lacking from the workplace. It will provide remote assistance to onboarding, training, collaboration, and improved diversity and inclusion, and it will keep employees who love working from home happy and engaged.
How will the metaverse change how B2B marketers reach new customers?
The metaverse is going to propel a new way of interacting among colleagues and enhance the capabilities of B2B marketing teams to better deliver immersive product experiences to potential customers. Marketers will be able to interact in real-time in a way that is more advanced and customizable than we've ever seen.
That will result in the metaverse helping marketing teams build more meaningful relationships with customers, as well as meet the customers where they choose to be. We'll see CX and marketing teams working closer together and their roles becoming more intertwined.
The metaverse can provide an enhanced layer of interactivity to...
1. Virtual conferences, demos, and tradeshows, beyond experiential and experimental fields
2. The way we interact with coworkers, allowing a virtual in-office experience
3. Business's ability to interact, market, and advertise in a more creative, strategic way so customers can connect more closely with the work environment (like going to an office in the past)
How can your sales and marketing team be metaverse-ready?
There is still so much unknown about to the metaverse, and it's difficult to imagine your coworkers seated in a virtual room all day bumping into avatars of other coworkers. But despite the skepticism, businesses should begin adapting to the future of work and how the metaverse will transform day-to-day "office" life.
For sales and marketing teams, the metaverse will be a place where you get your training, meet your colleagues, and get ahold of resources. Companies that see it as an opportunity to push the boundaries of operating will reap the benefits of building connection, community, and interaction amongst employees and customers like never before.
More Resources on the Metaverse and the Future of Marketing
What People Think of the Metaverse [Infographic]
A Second Look at Second Life
How to Prepare for Marketing's Flexible Future: Automated Marketing Processes
Robert Henderson is a co-founder and the CEO of JumpCrew, a sales and marketing agency that partners with B2B companies to accelerate their customer acquisition.
LinkedIn: Robert Henderson
Marketing Strategy Articles
You may like these other MarketingProfs articles related to Marketing Strategy:
The Attention Economy—How Time Affects Your B2B Marketing Efforts: Doug Binder on Marketing Smarts [Podcast]
What Keeps Senior Marketers Up at Night?
Inclusive B2B Marketing Techniques You Can't Afford to Ignore: Sydni Craig-Hart on Marketing Smarts [Podcast]
Three Predictions for B2B Marketing in 2023
The Future of SaaS Sales Lies in Interactive Demos and Product-Led Growth
The Top Strategies B2B Marketers Plan to Explore in 2023


Taco Daddy is the perfect place you would love to discover with friends. The ambiance and vibe draws you in, the food blows you away and the cocktails are absolutely amazing.
Our menu ranges from perfectly prepared plate of street-style carne asada tacos to award-winning barbecue tacos with sweet corn fresh tomato salsa. And what pairs better with an authentic Mexican dish than unforgettable margaritas, sangria, ice cold Mexican beers, and dozens of rare tequilas? Nothing!


JOHANNESBURG (AFP) - Lesotho Prime Minister Tom Thabane confirmed Saturday that the military had seized power in a coup in the tiny kingdom and that he had fled to neighbouring South Africa in fear of his life.
"I have been removed from control not by the people but by the armed forces, and that is illegal," Thabane told the BBC.
"I came into South Africa this morning and I will return as soon as my life is not in danger," he said. "I will not go back to Lesotho to get killed."
Lesotho's military seized control of police headquarters and the premier's residence in the capital Maseru in the early hours of Saturday, but later withdrew, a government minister told AFP.
"The armed forces, the special forces of Lesotho, have taken the headquarters of the police," said sports minister and leader of the Basotho National Party, Thesele Maseribane.
"The (military) commander said he was looking for me, the prime minister and the deputy prime minister to take us to the king. In our country, that means a coup," he said.
The putsch comes just months after a power struggle in the landlocked country that describes itself as the "kingdom in the sky".
Maseribane said people with guns were roaming the city but that he had no information about casualties, accusing the military of jamming radio stations and phone networks.
He accused Deputy Prime Minister Mothetjoa Metsing, leader of coalition partner Lesotho Congress for Democracy (LCD), of involvement in the move to seize power.
"There is some intelligence that he is part (of the coup)," he said.
The LCD is part of a shaky coalition which has governed since elections two years ago.
But, increasingly frustrated with Thabane, the party vowed months ago to form a new government and oust the premier in the nation that is entirely surrounded by South Africa.
In response, Thabane suspended parliament - with the blessing of King Letsie III who has ruled the constitutional monarchy since 1996 - allowing him to dodge a no-confidence vote.
After emergency talks in June, the coalition parties, including Thabane's All Basotho Convention (ABC), agreed to continue working together.
The sports minister said later Saturday that the military had moved away from the police headquarters and and returned to barracks, but that they had seized all police vehicles.
He had earlier insisted Thabane's government was still in control.
An AFP photographer reported shots ringing out in the early hours, saying a reinforced military contingent was guarding the prime minister's official residence and that soldiers were patrolling the streets of Maseru.
Maseribane said he had fled his residence after receiving a warning about an impending putsch, and refused to divulge his whereabouts.
"The prime minister and myself, (we are) still the coalition government. The prime minister is still in power," he said.
"There's still a lot of danger. People who have arms are running around Maseru." Metsing could not immediately be reached for comment, but another LCD member, Communications Minister Selibe Mochoboroane, denied knowledge of events in the capital.
"I've just heard now," he told AFP, speaking from the countryside.
Two clerics who were part of the team that mediated the coalition deal in June said they were rushing to the capital.
"Pray for our country, we don't know what is happening," Lesotho Evangelical Church head Simeon Masemene told AFP.
In 1986, South Africa's apartheid government instigated a coup to prevent the country being used as a base by the African National Congress and other activists.
In recent decades there has been a series of attempted political assassinations.
But the last elections in 2012 passed off relatively peacefully, with three major parties forging a coalition.
However coalition partners have accused Thabane of operating without consulting them.
"Since the previous elections, the coalition struggles to work and the premier was criticised for his authoritarianism," a European diplomatic source in Lesotho told AFP.
The power tussle had drawn concern from powerful neighbour South Africa, which gets water and electricity from the kingdom.