text:
Bacterial microcompartment
Stylized view of the carboxysome and related bacterial structures such as the propanediol utilization (Pdu) and ethanolamine utilization (Eut) microcompartments. Distinct hexameric BMC shell proteins carrying out different functions in the shell are shown in different shades of blue. Pentameric vertex proteins are shown in magenta. Encapsulated enzymes are shown in green, organized in layers. [Image: T. Yeates]
Bacterial microcompartments (BMCs) are organelle-like structures, consisting of a protein shell that encloses enzymes and other proteins. BMCs are typically about 40–200 nanometers in diameter and are entirely made of proteins.[1][2][3][4][5][6][7] The shell functions like a membrane, as it is selectively permeable.[2][4][6][8][9] Other protein-based compartments found in bacteria and archaea include encapsulin nanocompartments[10] and gas vesicles.[11]
1 Discovery
2 Shells
2.1 Protein families forming the shell
3 The BMC shell protein family
3.1 Single-domain proteins (BMC-H)
3.2 Tandem-domain proteins (BMC-T)
3.3 The EutN/CcmL family (BMC-P)
4 Origin of BMC and relation to viral capsids
5 Permeability of the shell
6.1 Carboxysomes: carbon fixation
6.2 Metabolosomes: aldehyde oxidation
6.2.1 PDU BMCs
6.2.2 EUT BMCs
6.2.3 Bifunctional PDU/EUT BMCs
6.2.4 Glycyl radical enzyme-containing BMCs (GRM)
6.2.5 Planctomycetes and Verrucomicrobia BMCs (PVM)
6.2.6 Rhodococcus and Mycobacterium BMCs (RMM)
6.2.7 BMCs of unknown function (BUF)
7 Assembly
7.1 Carboxysomes
7.2 Metabolosomes
8 Regulation (genetic)
9 Relevance to global and human health
10 Biotechnological applications
Discovery[edit]
Further information: Carboxysome
The first BMCs were observed in the 1950s in electron micrographs of cyanobacteria,[12] and were later named carboxysomes after their role in carbon fixation was established.[13] Until the 1990s, carboxysomes were thought to be an oddity confined to certain autotrophic bacteria. But then genes coding for proteins homologous to those of the carboxysome shell were identified in the pdu (propanediol utilization)[14] and eut (ethanolamine utilization)[15] operons. Subsequently, transmission electron micrographs of Salmonella cells grown on propanediol[16] or ethanolamine[17] showed the presence of polyhedral bodies similar to carboxysomes. The term metabolosome is used to refer to such catabolic BMCs (in contrast to the autotrophic carboxysome).
Although the carboxysome, propanediol utilizing (PDU), and ethanolamine utilizing (EUT) BMCs encapsulate different enzymes and therefore have different functions, the genes encoding for the shell proteins are very similar. Most of the genes (coding for the shell proteins and the encapsulated enzymes) from experimentally characterized BMCs are located near one another in distinct genetic loci or operons. There are currently over 20,000 bacterial genomes sequenced, and bioinformatics methods can be used to find all BMC shell genes and to look at what other genes are in the vicinity, producing a list of potential BMCs.[6][18][19] In 2014, a comprehensive survey identified 23 different loci encoding up to 10 functionally distinct BMCs across 23 bacterial phyla.[19]
Shells[edit]
Protein families forming the shell[edit]
The BMC shell appears icosahedral or quasi-icosahedral, and is formed by (pseudo)hexameric and pentameric protein subunits.
The three types of proteins (BMC-H, BMC-T and BMC-P) known to form the shell of BMCs. The encapsulated enzymes/proteins (shown in purple, red and turquoise) constitute a metabolic reaction sequence. (Image credit: Seth Axen, Markus Sutter, Sarah Newnham, Clement Aussignargues and Cheryl Kerfeld)
The BMC shell protein family[edit]
Main article: BMC domain
The major constituents of the BMC shell are proteins containing Pfam00936 domain(s). These proteins form oligomers that are hexagonal in shape and are thought to form the facets of the shell.[2][20][21]
Single-domain proteins (BMC-H)[edit]
The BMC-H proteins, which contain a single copy of the Pfam00936 domain, are the most abundant component of the facets of the shell. The crystal structures of a number of these proteins have been determined, showing that they assemble into cyclical hexamers, typically with a small pore in the center.[2] This opening is proposed to be involved in the selective transport of the small metabolites across the shell.
Tandem-domain proteins (BMC-T)[edit]
A subset of shell proteins are composed of tandem (fused) copies of the Pfam00936 domain (BMC-T proteins). The structurally characterized BMC-T proteins form trimers that are pseudohexameric in shape.[22][23][24] Some BMC-T crystal structures show that the trimers can stack in a face-to-face fashion. In such structures, one pore from one trimer is in an "open" conformation, while the other is closed – suggesting that there may be an airlock-like mechanism that modulates the permeability of some BMC shells.[22][25] Another subset of BMC-T proteins contain a [4Fe-4S] cluster, and may be involved in electron transport across the BMC shell.[26][27][28][29][30]
The EutN/CcmL family (BMC-P)[edit]
Twelve pentagonal units are necessary to cap the vertices of an icosahedral shell. Crystal structures of proteins from the EutN/CcmL family (Pfam03319) have been solved and they typically form pentamers (BMC-P).[31][32][33] The importance of the BMC-P proteins in shell formation seems to vary among the different BMCs. It was shown that they are necessary for the formation of the shell of the PDU BMC as mutants in which the gene for the BMC-P protein was deleted cannot form shells,[34] but not for the alpha-carboxysome: without BMC-P proteins, carboxysomes will still assemble and many are elongated; these mutant carboxysomes appear to be "leaky".[35]
Origin of BMC and relation to viral capsids[edit]
While the BMC shell is architecturally similar to many viral capsids, the shell proteins have not been found to have any structural or sequence homology to capsid proteins. Instead, structural and sequence comparisons suggest that both BMC-H (and BMC-T) and BMC-P, most likely, have evolved from bona fide cellular proteins, namely, PII signaling protein and OB-fold domain-containing protein, respectively.[36]
Permeability of the shell[edit]
It is well established that enzymes are packaged within the BMC shell and that some degree of metabolite and cofactor sequestration must occur.[4] However, other metabolites and cofactors must also be allowed to cross the shell in order for BMCs to function. For example, in carboxysomes, ribulose-1,5-bisphosphate, bicarbonate, and phosphoglycerate must cross the shell, while carbon dioxide and oxygen diffusion is apparently limited.[37][38] Similarly, for the PDU BMC, the shell must be permeable to propanediol, propanol, propionyl-phosphate, and potentially also vitamin B12, but it is clear that propionaldehyde is somehow sequestered to prevent cell damage.[39] There is some evidence that ATP must also cross some BMC shells.[4]
It has been proposed that the central pore formed in the hexagonal protein tiles of the shell are the conduits through which metabolites diffuse into the shell.[2][20] For example, the pores in the carboxysome shell have an overall positive charge, which has been proposed to attract negatively charged substrates such as bicarbonate.[2][4][9][20] In the PDU microcompartment, mutagenesis experiments have shown that the pore of the PduA shell protein is the route for entry of the propanediol substrate.[40] For larger metabolites, a gating mechanism in some BMC-T proteins is apparent.[22][25][41] In the EUT microcompartment, gating of the large pore in the EutL shell protein is regulated by the presence of the main metabolic substrate, ethanolamine.[42]
The presence of iron-sulfur clusters in some shell proteins, presumably in the central pore, has led to the suggestion that they can serve as a conduit through which electrons can be shuttled across the shell.[26][29][30]
Types[edit]
A recent comprehensive survey of microbial genome sequence data indicated up to ten different metabolic functions encapsulated by BMC shells.[19] The majority are involved in either carbon fixation (carboxysomes) or aldehyde oxidation (metabolosomes).[19]
Generalized function schematic for experimentally characterized BMCs. (A) Carboxysome. (B) Metabolosome. Reactions in gray are peripheral reactions to the core BMC chemistry. BMC shell protein oligomers are depicted on the left: blue, BMC-H; cyan, BMC-T; yellow, BMC-P. 3-PGA, 3-phosphoglycerate, and RuBP, ribulose 1,5-bisphosphate.[19]
Carboxysomes: carbon fixation[edit]
Main article: Carboxysome
Electron micrographs showing alpha-carboxysomes from the chemoautotrophic bacterium Halothiobacillus neapolitanus: (A) arranged within the cell, and (B) intact upon isolation. Scale bars indicate 100 nm.[20]
Carboxysomes encapsulate ribulose-1,5-bisphosphate carboxylase/oxygenase (RuBisCO) and carbonic anhydrase in carbon-fixing bacteria as part of a carbon concentrating mechanism.[43] Bicarbonate is pumped into the cytosol and diffuses into the carboxysome, where carbonic anhydrase converts it to carbon dioxide, the substrate of RuBisCO. The carboxysome shell is thought to be only sparingly permeable to carbon dioxide, which results in an effective increase in carbon dioxide concentration around RuBisCO, thus enhancing carbon fixation.[38][44] Mutants that lack genes coding for the carboxysome shell display a high carbon requiring phenotype due to the loss of the concentration of carbon dioxide, resulting in increased oxygen fixation by RuBisCO. The shells have also been proposed to restrict the diffusion of oxygen,[9][38] thus preventing the oxygenase reaction, reducing wasteful photorespiration.[37]
Electron micrograph of Synechococcus elongatus PCC 7942 cell showing the carboxysomes as polyhedral dark structures. Scale bar indicates 500 nm. (Image credit: Raul Gonzalez and Cheryl Kerfeld)
Metabolosomes: aldehyde oxidation[edit]
In addition to the anabolic carboxysomes, several catabolic BMCs have been characterized that participate in the heterotrophic metabolism via short-chain aldehydes; they are collectively termed metabolosomes.[4][17]
These BMCs share a common encapsulated chemistry driven by three core enzymes: aldehyde dehydrogenase, alcohol dehydrogenase, and phosphotransacylase.[4][19][45] Because aldehydes can be toxic to cells[39] and/or volatile,[46] they are thought to be sequestered within the metabolosome. The aldehyde is initially fixed to coenzyme A by a NAD+-dependent aldehyde dehydrogenase, but these two cofactors must be recycled, as they apparently cannot cross the shell.[47][48] These recycling reactions are catalyzed by an alcohol dehydrogenase (NAD+),[47] and a phosphotransacetylase (coenzyme A),[48] resulting in a phosphorylated acyl compound that can readily be a source of substrate-level phosphorylation or enter central metabolism, depending on if the organism is growing aerobically or anaerobically.[39] It seems that most, if not all, metabolosomes utilize these core enzymes. Metabolosomes also encapsulate another enzyme that is specific to the initial substrate of the BMC, that generates the aldehyde; this is considered the signature enzyme of the BMC.[4][19]
PDU BMCs[edit]
Electron micrograph of Escherichia coli cell expressing the PDU BMC genes (left), and purified PDU BMCs from the same strain (right). (Image credit: Joshua Parsons, Steffanie Frank and Martin Warren)
Some bacteria can use 1,2-propanediol as a carbon source. They use a BMC to encapsulate several enzymes used in this pathway (Sampson and Bobik, 2008). The PDU BMC is typically encoded by a 21 gene locus. These genes are sufficient for assembly of the BMC since they can be transplanted from one type of bacterium to another, resulting in a functional metabolosome in the recipient.[28] This is an example of bioengineering that likewise provides evidence in support of the selfish operon hypothesis.[49] 1,2-propanediol is dehydrated to propionaldehyde by propanediol dehydratase, which requires vitamin B12 as a cofactor.[50] Propionaldehyde causes DNA mutations and as a result is toxic to cells, possibly explaining why this compound is sequestered within a BMC.[39] The end-products of the PDU BMC are propanol and propionyl-phosphate, which is then dephosphorylated to propionate, generating one ATP. Propanol and propionate can be used as substrates for growth.[39]
EUT BMCs[edit]
Ethanolamine utilization (EUT) BMCs are encoded in many diverse types of bacteria.[19] Ethanolamine is cleaved to ammonia and acetaldehyde through the action of ethanolamine-ammonia lyase, which also requires vitamin B12 as a cofactor.[51] Acetaldehyde is fairly volatile, and mutants deficient in the BMC shell have been observed to have a growth defect and release excess amounts of acetaldehyde.[46] It has been proposed that sequestration of acetaldehyde in the metabolosome prevents its loss by volatility.[46] The end-products of the EUT BMC are ethanol and acetyl-phosphate. Ethanol is likely a lost carbon source, but acetyl-phosphate can either generate ATP or be recycled to acetyl-CoA and enter the TCA cycle or several biosynthetic pathways.[17]
Bifunctional PDU/EUT BMCs[edit]
Some bacteria, especially those in the genus Listeria, encode a single locus in which genes for both PDU and EUT BMCs are present.[19] It is not yet clear whether this is truly a chimeric BMC with a mixture of both sets of proteins, or if two separate BMCs are formed.
Glycyl radical enzyme-containing BMCs (GRM)[edit]
Several different BMC loci have been identified that contain glycyl radical enzymes,[18][19] which obtain the catalytic radical from the cleavage of s-adenosylcobalamin.[52] One GRM locus in Clostridium phytofermentans has been shown to be involved in the fermentation of fucose and rhamnose, which are initially degraded to 1,2-propanediol under anaerobic conditions. The glycyl radical enzyme is proposed to dehydrate propanediol to propionaldehyde, which is then processed in a manner identical to the canonical PDU BMC.[53]
Planctomycetes and Verrucomicrobia BMCs (PVM)[edit]
Distinct lineages of Planctomycetes and Verrucomicrobia encode a BMC locus. The locus in Planctomyces limnophilus has been shown to be involved in the aerobic degradation of fucose and rhamnose. An aldolase is thought to generate lactaldehyde, which is then processed through the BMC, resulting in 1,2-propanediol and lactyl-phosphate.[45]
Rhodococcus and Mycobacterium BMCs (RMM)[edit]
Two types of BMC loci have been observed in members of the Rhodococcus and Mycobacterium genera, although their actual function has not been established.[19] However, based on the characterized function of one of the genes present in the locus and the predicted functions of the other genes, it was proposed that these loci could be involved in the degradation of amino-2-propanol. The aldehyde generated in this predicted pathway would be the extremely toxic compound methylglyoxal; its sequestration within the BMC could protect the cell.[19]
BMCs of unknown function (BUF)[edit]
One type of BMC locus does not contain RuBisCO or any of the core metabolosome enzymes, and has been proposed to facilitate a third category of biochemical transformations (i.e. not carbon fixation or aldehyde oxidation).[19] The presence of genes predicted to code for amidohydrolases and deaminases could indicate that this BMC is involved in the metabolism of nitrogenous compounds.[19]
Assembly[edit]
Carboxysomes[edit]
The assembly pathway for beta-carboxysomes has been identified, and begins with the protein CcmM nucleating RuBisCO.[54] CcmM has two domains: an N-terminal gamma-carbonic anhydrase domain followed by a domain consisting of three to five repeats of RuBisCO small-subunit-like sequences.[55] The C-terminal domain aggregates RuBisCO, likely by substituting for the actual RuBisCO small subunits in the L8-S8 holoenzyme, effectively cross-linking the RuBisCO in the cell into one large aggregate, termed the procarboxysome.[54] The N-terminal domain of CcmM physically interacts with the N-terminal domain of the CcmN protein, which, in turn, recruits the hexagonal shell protein subunits via an encapsulation peptide on its C-terminus.[56] Carboxysomes are then spatially aligned in the cyanobacterial cell via interaction with the bacterial cytoskeleton, ensuring their equal distribution into daughter cells.[57]
Alpha-carboxysome assembly may be different than that of beta-carboxysomes,[58] as they have no proteins homologous to CcmN or CcmM and no encapsulation peptides. Empty carboxysomes have been observed in electron micrographs.[59] Some micrographs indicate that their assembly occurs as a simultaneous coalescence of enzymes and shell proteins as opposed to the seemingly stepwise fashion observed for beta-carboxysomes. The formation of simple alpha-carboxysomes in heterologous systems has been shown to require just Rubisco large and small subunits, the internal anchoring protein CsoS2 and the major shell protein CsoS1A [60].
Metabolosomes[edit]
Metabolosome assembly is likely similar to that of the beta-carboxysome,[4][54] via an initial aggregation of the proteins to be encapsulated. The core proteins of many metabolosomes aggregate when expressed alone.[61][62][63][64] Moreover, many encapsulated proteins contain terminal extensions that are strikingly similar to the C-terminal peptide of CcmN that recruits shell proteins.[56][65] These encapsulation peptides are short (about 18 residues) and are predicted to form amphipathic alpha-helices.[56] Some of these helices have been shown to mediate the encapsulation of native enzymes into BMCs, as well as heterologous proteins (such as GFP).[56][66][67][68][69]
Regulation (genetic)[edit]
With the exception of carboxysomes, in all tested cases, BMCs are encoded in operons that are expressed only in the presence of their substrate.
PDU BMCs in Salmonella enterica are induced by the presence of propanediol or glycerol under anaerobic conditions, and only propanediol under aerobic conditions.[70] This induction is mediated by the global regulator proteins Crp and ArcA (sensing cyclic AMP and anaerobic conditions respectively),[71] and the regulatory protein PocR, which is the transcriptional activator for both the pdu and the cob loci (the operon necessary for the synthesis of vitamin B12, a required cofactor for propanediol dehydratase).[70]
EUT BMCs in Salmonella enterica are induced via the regulatory protein EutR by the simultaneous presence of ethanolamine and vitamin B12, which can happen under aerobic or anaerobic conditions. Salmonella enterica can only produce endogenous vitamin B12 under anaerobic conditions, although it can import cyanobalamin and convert it to vitamin B12 under either aerobic or anaerobic conditions.[72]
PVM BMCs in Planctomyces limnophilus are induced by the presence of fucose or rhamnose under aerobic conditions, but not by glucose.[45] Similar results were obtained for the GRM BMC from Clostridium phytofermentans, for which both sugars induce the genes coding for the BMC as well as the ones coding for fucose and rhamnose dissimilatory enzymes.[53]
In addition to characterized regulatory systems, bioinformatics surveys have indicated that there are potentially many other regulatory mechanisms, even within a functional type of BMC (e.g. PDU), including two-component regulatory systems.[19]
Relevance to global and human health[edit]
Carboxysomes are present in all cyanobacteria and many other photo- and chemoautotrophic bacteria. Cyanobacteria are globally significant drivers of carbon fixation, and since they require carboxysomes to do so in current atmospheric conditions, the carboxysome is a major component of global carbon dioxide fixation.
Several types of BMCs have been implicated in virulence of pathogens, such as Salmonella enterica and Listeria monocytogenes. BMC genes tend to be upregulated under virulence conditions, and mutating them leads to a virulence defect as judged by competition experiments.[73][74][75][76][77]
Biotechnological applications[edit]
Several features of BMCs make them appealing for biotechnological applications. Because carboxysomes increase the efficiency of carbon fixation, much research effort has gone into introducing carboxysomes and required bicarbonate transporters into plant chloroplasts in order to engineer a chloroplastic CO2 concentrating mechanism[78][79] with some success [60].
More generally, because BMC shell proteins self-assemble, empty shells can be formed,[34][69] prompting efforts to engineer them to contain customized cargo. Discovery of the encapsulation peptide on the termini of some BMC-associated proteins[56][66] provides a means to begin to engineer custom BMCs by fusing foreign proteins to this peptide and co-expressing this with shell proteins. For example, by adding this peptide to pyruvate decarboxylase and alcohol dehydrogenase, researchers have engineered an ethanol bioreactor.[80] Finally, the pores present in the shell proteins control the permeability of the shell: these can be a target for bioengineering, as they can be modified to allow the crossing of selected substrates and products.[81]
Endomembrane system
Substrate channeling
Encapsulins
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Mysterious Bacterial Microcompartments Revealed By Biochemists
Not so simple after all. A renaissance of research into prokaryotic evolution and cell structure
Retrieved from "https://en.wikipedia.org/w/index.php?title=Bacterial_microcompartment&oldid=929675040"
Bacterial proteins


Lauren! Thanks for letting me live vicariously thru you for the last 10 months while I've been away from Mongolia. I know your doco will be rockin and I can't wait to see it. Enjoy life back in the land of salads, road rules and good old American language. Hope to see you soon and keep writing!!


text:
Q: Calculate $\lim _{x\to 0^+}\frac{\left(e^x-e^{-x}\right)}{\sin x}$ ***How to find the this limit without using L'Hopital's Rule.
$\lim _{x\to 0^+}\frac{\left(e^x-e^{-x}\right)}{\sin x}$

A: Hint:

*

*Use maclaurin series for $e^x$ and $e^{-x}$

*then apply $$\lim_{x\to 0} \dfrac{\sin x}{x}=1$$

A: Two famous limits give it as$$\lim_{x\to0^+}\frac{x}{\sin x}\left(\frac{e^x-1}{x}+\frac{e^{-x}-1}{-x}\right)=1(1+1)=2.$$

redpajama_set_name: RedPajamaStackExchange


The former School for Young Ladies (1887, Giacomo Zammattio) opposite the Hotel Bonavia was converted into the Scientific Library in 1948, and the University Library in 1979. The main reason to visit is the permanent exhibition of the Glagolitic script. One of the leading collections of this kind in the world, on display are replicas of stone tablets written in this ancient Slavic alphabet, including the Baška tablet from Krk island, one of the most important document of this kind in existence. Together with frescoes, masonry, manuscripts, books and paintings, this exhibition is truly an opportunity to see something very beautiful and very unique to Croatia. Call to make an appointment to view – it's well worth it.
Open Mon - Fri 08:00 - 14:00 with prior arrangement.


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FLEXNER v. FARSON
FLEXNER v. FARSON , 248 U.S. 289 (1919)
FLEXNER v. FARSON(1919)
Argued: Decided: January 7, 1919
Mr. J. S. Laurent, of Louisville, Ky., for plaintiff in error.[ Flexner v. Farson 248 U.S. 289 (1919) ]
[248 U.S. 289, 292] Messrs. Harry P. Weber and George W. Miller, both of Chicago, Ill., for defendants in error.
Mr. Justice HOLMES delivered the opinion of the Court.
This is an action brought by the plaintiff in error upon a judgment for money rendered by a Kentucky Court. The declaration alleges that the transaction in respect of which the judgment was rendered took place at Louisville, Kentucky, and that at that time the defendants were doing business there as partners through Washington Flexner, who was and continued to be their agent until the time of this suit. It further alleges that the defendants were non-residents and that the service of summons of the Kentucky suit was made upon Washington Flexner in accordance with a Kentucky statute (Civ. Code Prac. 51) authorizing it to be made in that way. The defendant William Farson was the only one served with process in the present action and he pleaded that the defendants in the former suit did not reside in Kentucky, were not served with process and did not appear; that Washington Flexner was not their agent at the time of service upon him; that the Kentucky statute relied upon was unconstitutional; that the Kentucky Court had no jurisdiction, and that its judgment was void under the Constitution of the United States. The plaintiff demurred to the pleas, and stood upon his demurrer when it was overruled, whereupon judgment was entered for the defendants. There was an appeal to the Supreme Court of the State on the ground that the Court below did not give full faith and credit to the Kentucky judgment and erred in holding the Kentucky statute as to service unconstitutional. The Supreme Court affirmed the judg [248 U.S. 289, 293] ment below. 268 Ill. 435, 109 N. E. 327, Ann. Cas. 1916D, 810. The same errors are alleged here.
It is argued that the pleas tacitly admit that Washington Flexner was agent of the firms at the time of the transaction sued upon in Kentucky, and the Kentucky statute is construed as purporting to make him agent to receive service in suits arising out of the business done in that State. On this construction it is said that the defendants by doing business in the State consented to be bound by the service prescribed. The analogy of suits against insurance companies based upon such service is invoked. Mutual Reserve Fund Life Association v. Phelps, 190 U.S. 147 , 23 Sup. Ct. 707. But the consent that is said to be implied in such cases is a mere fiction, founded upon the accepted doctrine that the States could exclude foreign corporations altogether, and therefore could establish this obligation as a condition to letting them in. Lafayette Ins. Co. v. French, 18 How. 404; Pennsylvania Fire Ins. Co. v. Gold Issue Mining & Milling Co., 243 U.S. 93, 96 , 37 S. Sup. Ct. 344. The State had no power to exclude the defendants and on that ground without going farther the Supreme Court of Illinois rightly held that the analogy failed, and that the Kentucky judgment was void. If the Kentucky statute purports to have the effect attributed to it, it cannot have that effect in the present case. New York Life Ins. Co. v. Dunlevy, 241 U.S. 518, 522 , 523 S., 36 Sup. Ct. 613

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text:
Edward Kennedy FBI Records Show Death Threats As Late As 1985
Andrew Miga and Glen Johnson, the Associated Press
WASHINGTON (AP) — FBI records show there were death threats against then-Sen. Edward Kennedy even five years after his failed 1980 White House bid.
Previously secret files released Monday showed that on May 23, 1985, the U.S. Capitol Police passed onto the FBI a copy of a letter sent to the Secret Service, ostensibly by a Warren, Mich., resident. The sender, whose name was redacted, declared: "Brass tacks, I'm gonna kill Kennedy and (President Ronald) Reagan, and I really mean it."
The FBI considered the sender armed and dangerous, but an accompanying psychological analysis said she was "merely ventilating her frustrations and projecting her inadequacies." The late Sen. Kennedy, who served in the Senate for nearly half a century, died in August 2009 after a yearlong struggle with brain cancer.
THIS IS A BREAKING NEWS UPDATE. Check back soon for further information. AP's earlier story is below.
WASHINGTON (AP) — Most of the secret FBI files on the late Sen. Edward Kennedy being released Monday concern death threats against the longtime senator.
Alex Brown of the FBI's records management division said the FBI would post some 2,000 pages of previously secret pages about the Massachusetts Democrat on the agency's website.
The release of the documents has been highly anticipated by historians, scholars and others interested in the life and long public career of one of America's most prominent and powerful politicians.
The Associated Press and other media organizations requested the documents through Freedom of Information Act requests.
Kennedy faced death threats when he ran for president in 1980 and before that in the years following the assassinations of his older brothers.
President John F. Kennedy was assassinated in Dallas on Nov. 22, 1963. U.S. Sen. Robert F. Kennedy was slain in Los Angeles on June 6, 1968.
The deaths of his two older brothers cast a long shadow on Kennedy's life, and prompted fears he too would be targeted by an assassin's bullet.
After his brothers' assassinations, Kennedy wrote in his memoir "True Compass" released last year, that he was easily startled at loud sounds, and would hit the deck whenever a car backfired.
Kennedy, who served in the Senate for nearly half a century, died in August 2009 after a yearlong struggle with brain cancer. He was 77 and the last surviving brother of the famed political family.
Read the files yourself here:
about-FBI
about-Federal-Bureau-of-Investigation
Oregon Jury Finds Boy Scouts Negligent in Sex Case
Washington Adoption Agency Suspended After Russian Scandal
Malcolm X Assassin Freed on Parole
Fourth New Orleans Police Officer Pleads Guilty in Shooting Cover-Up
FBI Agrees to Probe Another New Orleans Police Department Shooting


text:
gaziantep museum (gaziantep, turkey) (2)
british museum (london, england, united kingdom) (1)
museo nazionale romano (rome, italy) (1)
staatliche museen preussischer kulturbesitz (berlin, germany) (1)
staatliche museen preussischer kulturbesitz, pergamonmuseum (berlin, germany) (1)
staatliche museen preussischer kulturbesitz, pergamonmuseum, antikensammlung (berlin, germany) (1)
phidias (greek sculptor, ca.500 - ca.432 b.c.) (1)
athens (greece) (2)
acropolis (athens, greece) (1)
pompeii (extinct city) (1)
rome (italy) (1)
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roman (ancient italian style) (4)
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imperial (roman) (3)
frescoes (paintings) (2)
mosaic pavements (2)
mural paintings (visual works) (2)
Title: Dionysus
House of Poseidon, Zeugma [Turkey], mosaic pavement, Triumph of Dionysus [Dionysos].
Roman (ancient Italian style); Imperial (Roman)
This mosaic "decorated the vertical bar of the T-form figured composition of the dining room floor to which the mosaic of Pasiphae and Daedalus belonged. The thick swastika-meander band in perspective at the top was the partition between the two...
Villa Farnesina, Rome, Italy, interior view, Bedroom B, rear wall, with inset of nymphs and infant Dionysus.
Roman (ancient Italian style); Augustan; Imperial (Roman); Early Imperial
"Painted wall with inset showing nymphs with the infant Dionysus / rear wall of Cubiculum 2 of the villa under the Farnesina" (caption)
Villa of the Mysteries, Pompeii, Italy, interior view, [Salon of the Mysteries] Room 5 (oecus), fresco detail, young Dionysus [Dionysos] and two priestesses.
Roman (ancient Italian style); Second Style
"The large oecus (5) next to the nuptial bedchamber (4) contains the famous frieze representing the "mysteries" of the Dionysus cult that give the villa its name. The paintings here represent the initiation of a young woman into the mysteries of...
House of Poseidon, Zeugma [Turkey], plan of T-form triclinium with Pasiphae and Daedalus and Triumph of Dionysus [Dionysos] mosaics.
The area outside these panels is covered with geometric mosaics of different patterns. (NOTE: For detailed descriptions of the individual mosaics, see the individual records for "Pasiphae and Daedalus" and "Triumph of Dionysus").
Parthenon (Temple of Athena Parthenos), Acropolis, Athens, Greece, east pediment, Helios, his horses, and Dionysos [Dionysus] (Herakles?).
Greek (ancient); Classical; High Classical; Phidian
Attic red-figure kylix, exterior view, ritual in honor of Dionysos [Dionysus].
Greek (ancient); Archaic (Greek); Attic (Mainland Greek pottery styles); Red-figure
From Vulci, [Italy].
Theater of Dionysus [Dionysos], Athens, Greece, reconstruction.
Greek (ancient); Classical
"The Sanctuary of Asclepius is at the bottom left." (Caption, p.101); "The new skene, which had three doorways in it, was fronted by a closed colonnade. It also had two wings projecting forward 5 metres (16 1/2 feet), which were fronted with an...


Stockist of: Acana, Applaws, Barking Heads, Burns, Canagan, Collards, Company of Animals, Lily's Kitchen, Orijen, Symply, Taste of the Wild.
The Petshop in Brigg, established in 1986. Specialising in premium goods for pets. Suppliers of Hunter, Hurtta, Animate and Outhwaite goods.


Every 10 seconds someone in the UK has a potentially lifethreatening asthma attack and three people die every day from the condition. Tragically, evidence shows two-thirds of these deaths could be prevented by using some key elements of basic care. Also, many of these deaths occur in people with mild or moderate asthma, the kind that can be managed in primary care and with daily self-management.


In the ecommerce world today, achieving a solid social media presence is just as crucial, or even more crucial than having a stunning website. With the right social media consultant, you'll have to worry about managing your own social media accounts.
Sayles Industries is a social media marketing agency that professionally manages social media channels to increase engagement, implement effectual lead generation campaigns and grow social presence all together!
Whether scheduling shares, creating content, repurposing content, community management, engaging with fans, or sharing others' content, as a Social Media Marketing and Management Agency, Sayles Industries helps budget-conscious business owners like you to achieve their marketing objectives with a big bang.
From our direct experience managing our own social media, we know small business owners new to social media marketing sometimes find it pretty overwhelming to juggle and manage their accounts at scale or run an agency effectively.
Using proven, smarter social media management and communication tools, we help you tap into the huge online prospects for better results in terms of broad online presence, customer engagement and conversion.
These days, social media has grown such that small businesses are not only solidifying their online presence on more powerful social media networks, but are also investing more dollars in these channels.
As a matter of fact, social media ads alone spent a whopping $8.5 billion in 2014, and this figure is expected to hit $14 billion by 2018. As one of the best social media management in Tri-State region of Pennsylvania and Erie, PA, Sayles Industries helps businesses of all sizes to launch successful social media marketing across the major social media channels.
As a qualified social media consultant, we have created and managed excellent social media campaigns for hundreds—and we're still counting, of small businesses throughout Erie, PA as well as Ohio and New York.
Sayles Industries specializes in social network management and can manage various channels including Facebook, Twitter, Instagram and Google Plus on your behalf. As a leader in social media monitoring in the greater Tri-State region of Pennsylvania, we use relevant social media management tools to ensure a strong online presence for your business.
Our social media strategies are tailored with your target audience in mind. They are clear-cut and well thought-out, enabling you to grow your business as well as meet your marketing goals.
Having worked closely with startups, we know for sure that the thought of spending money on paid social can sometimes feel unnerving for many small business owners.
Given the increased number of features, possibilities and social networks, paid social isn't the only expense associated with effective social media marketing. Creating fresh and engaging content and executing a full-blown strategy also costs time.
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Named after the city in which it is located, Crystal Airport also sits adjacent to Brooklyn Park and Brooklyn Center. The airport currently has three paved and one turf runway and two non-precision instrument approaches. Runway 14L-32R is 3,263' x 75'; Runway 14R-32L is 3,266' x 75'; and Runway 6L-24R is 2,499' x 75'. Closed during the winter months, turf Runway 6R-24L is 2,122' x 150'. A fixed-base operator is on site, as is an FAA-operated air traffic control tower, which operates daily in winter from 7 a.m. to 9 p.m. and in summer from 7 a.m. to 10 p.m.
Crystal Airport has a total annual economic output of $71 million and supports 320 jobs, including 100 directly tied to on-airport businesses.
There are 168 aircraft based at Crystal Airport and in 2018, there were 38,109 landings and takeoffs.
The Crystal Airport 2035 LTCP has been finalized and can be downloaded at the links below. Volume 1 contains the report; Volume 2 contains the appendices, including the public comments (and responses) received as part of the community and stakeholder engagement process. The documents are in PDF format and require Adobe Reader software to read or download.
Archived documents associated with the Crystal Airport planning process can be found here.


Download our Maternity Registration and Agreement Info HERE.
Download our Normal Registration and Agreement Info HERE.
Kindly fax or e-mail the completed forms to us, together with proof of payment.
Mom's Link will supply the forms as well as step-by-step instructions on how to complete each form.
Please contact our office for the most recent forms.
Download our Registration and Agreement Info.
Upon receipt of your registration and proof of payment, you receive an Information pack, consisting of all necessary forms and relevant information for a successful claim.
Once your forms have been completed, fax or e-mail the completed forms to Mom's Link to proofread and advise you of any incomplete information.
Post, Courier or deliver the original completed forms to us.
We submit your initial application and monthly claims to the Department of Labour for the duration of your claim period.
UIF Benefit is paid directly into your bank account.
attend to your little Baby and Dad.


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Vehicle Traveller
A site with all the info about mechanized travell from traffic light to traffic light to global expeditions to racing information
Posted November 10, 2018 by Vehicle Traveller	Car Racing
Kubica and Williams
http://www.pitpass.com/63468/Kubica-and-Williams
It was reported yesterday that Robert Kubica is "in the frame" for the seat alongside George Russell at Williams next season, indeed it was claimed he has a "race drive on offer".
"I think we are quite close to the decision," the Pole told Motorsport.com. "From my point of view I'm getting there, and I have a deadline very soon, in my head let's say.
"It will be within a few days, what I decide, what I want to do," he added, "and what I think is the best direction for me. I'm in a comfortable situation, and this is what I've been saying for a few weeks. I will be doing something which in one way or another attracts me, and gives me the confidence that I will be doing something that I enjoy. But for sure a lot depends on making my mind up on what direction I want to go, if I want to race, and where to race, if I can combine things, and if I can focus only on one thing, as I did this year. As I said, I have my deadline, which I will respect, which is in the next few days. Then we will see."
The Pole's determination to return to the sport following his almost fatal rallying crash in 2011 is the stuff of legend, and his disappointment on missing out on the seat at Williams this year was only matched by the disappointment of his many fans and admirers.
However, muddying the waters is talk of the Pole joining Ferrari as a development driver, the Italian team having lost Daniil Kvyat to Toro Rosso and Antonio Giovinazzi to Sauber.
Ferrari places much emphasis on its development drivers whose simulator work over Grand Prix weekends is known to have turned the team's fortunes around on a number of occasions over the last few years.
However, Ferrari being Ferrari, it is unlikely that a development role – no matter how significant – will lead to a full race seat with the Maranello outfit, somewhat ironic when you consider that he had agreed a deal to race for the Maranello outfit in 2012 prior to his 2011 rally crash.
While a decent performance for Ferrari might lead to a placement at Haas or Sauber, this could be a couple of years away and the Pole is already 33.
Then, we are told, he is "in the frame" at Williams, however, as we know from experience that is no guarantee.
Indeed, our sources claim that the loss of potential sponsor Rich Energy to Haas was a far bigger blow to the Grove outfit than many realised, with the team going to extraordinary efforts (and cost) to secure the deal. Indeed, we understand that a 2 am call to reveal the Haas decision left team boss Claire Williams in tears.
Consequently, it would appear that the Grove outfit needs a driver who can bring a substantial amount of money to the team, and Kubica simply doesn't have it.
A job-share – what with Williams being powered by Mercedes – is totally out of the question, therefore the Ferrari development role appears to be Kubica's only genuine prospect.
Whether he genuinely believes the Williams seat is a real prospect – knowing something the rest of us don't – Kubica admits that when it comes to priorities he remains undecided, though he understandably appears to favour the prospect of a short-term racing position than a longer-term 'back office' role with Ferrari.
"Maybe the wish of driving and coming back to F1 is bigger than the wish of a long project," he says. "I leave a lot to personal conclusions. But the final conclusion is my one, and I will make it.
"When I'm saying I want to make my mind up, it's also about what I want to do with my future," he adds. "Definitely I'm not looking only for the next three months, or one year, but what's is my feeling. Not everything depends on my feeling, it's not because once I decide everybody is waiting with open arms, there are also things to look at and see how it can work. I have a long flight back from Brazil, it's good to have last thoughts, and then we'll see."
Nonetheless, the Pole admits that a job with Ferrari would appeal.
"I said always when you are a small child you dream about F1, then you once you are established as an F1 driver there are two things, either you win championships, or you drive in the red car. I was quite close to doing it, it didn't work out.
"I cannot look behind, I have to look forward," he adds. "It could be very interesting, but I have to see more about working with a top team on a high level. It would be a good opportunity from a professional point of view, but also from an emotional point of view it can be something interesting."
Check out our Friday gallery from Interlagos, here.
via Pitpass – the latest hottest F1 news http://www.pitpass.com/
November 10, 2018 at 11:36AM
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Vehicle Traveller Kubica and Williams


HELSINGIN SANOMAT SENDS A WORM TO BETHLEHEM FOR CHRISTMAS, A ROTTEN REPORT ENSUES …… – The Tundra Tabloids…….
Da Jooos did dis, and da Jooos did dat, and da poor Palestians did nothing but be wictims. End of da report.
The article is a textbook example of how the journalists twist the truth to suit their agenda.
1. In the beginning, state the comfortable facts, omit the uncomfortable ones. Don't go overboard yet.
2. In the end, introduce the big lie. Don't say it yourself, quote a local professional propagandist. Make him (or her in this case) look like a perfect representative of a persecuted minority (though she happens to be the mayor of Bethlehem and has Arafat and Abbas pictures hanging on the wall).
3. Don't introduce any background, let the readers believe the big lie. It's the Jews' fault.
One of the central themes in the tawdry piece was insistence that the depletion of the Christian population in Bethlehem was solely due to Israel's defensive security fence/wall (and other security measure) that snakes through the many areas of Bethlehem. Hey, they even got an Arab Lutheran pastor to state it, so it's got to be true!
And where are all the Christians of Bethlehem?
When Israel declared its independence in 1948, Bethlehem's inhabitants were up to 85 per Christian. Today, Christians are a 25 percent minority.
"Nobody will give you actual census figures, because then they'd have a lot of explaining to do," he said.
"The percentages are what's important. The percentage, if you went back to 1948, maybe 80% of the population of Bethlehem was Christian, more or less. It declined precipitously during the Jordanian 20 years [1949-67] and that puts the lie to the implication that it's all Israel's fault.
Some Israeli politicians have argued that the mass exodus of Christians is caused by Muslim persecution.
This is a blatant lie, say Babu and pastor Raheb.
"Extremist Jews and Christian Zionists use the Palestinian Christians stick horse to justify islamkammoaan" Raheb says.
But Huusko and the Helsingin Sanomat were not after the facts, just the narrative that they want to import to their ever dwindling list of subscribers, so of course Prof.Justus Reid Weiner, a man who has spent years in highlighting the plight of Christian Arab under Fatah and Hamas rule, was not consulted for his opinions on anything.
NOTE: Huusko the worm was in the Helsinki University auditorium during the Avi Shlaim seminar, during which time the then Israeli ambassador, Avi Granot, delivered the following wise words of advice. Huusko the worm was seen sitting up towards the back, check at the 13 second mark whose head can be seen behind the man Amb.Granot was speaking to.
Previous Post Previous Post DR.MANFRED GERSTENFELD: GENOCIDE OF THE JEWS, HAMAS WORSE THAN ISLAMIC STATE…….


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Pennsylvania Governors Residences Open to the Public
Written by PA Heritage Staff in the News category and the Winter 2014 issue Topics in this article: Abraham Lincoln, American Civil War, American Revolution, Andrew Gregg Curtin, architecture and architects, Arthur H. James, Battle of Germantown, Bucks County, Colonial Revival, Cornelia Bryce Pinchot, David L. Lawrence, Delaware River, Edward Martin (governor), Fort Indiantown Gap, George M. Leader, George Washington, Georgian style, Gifford Pinchot, Graeme Park, Grey Towers, Hannah Callowhill Penn, Harrisburg, Horsham, James H. Duff, James Pinchot, John C. Bell, John F. Kennedy, Margaret Pennypacker, Mary Jane Eno Pinchot, Milford, Montgomery County, Morrisville, National Historic Landmark, National Park Service, National Register of Historic Places, New York Times, Pennsbury Manor, Pennsylvania General Assembly, Pennsylvania Historical and Museum Commission, Pennsylvania National Guard, Pennsylvania State House, Pennsylvania State Police, Pennypacker Mills, Perkiomen Creek, Philadelphia, Pike County, Raymond P. Shafer, Richard Morris Hunt, Samuel W. Pennypacker, Schwenksville, Susquehanna River, Thomas Graeme, U.S. Forest Service, William Keith, William Penn, World War II
News presents briefs about current and forthcoming programs, events, exhibits and activities of historical and cultural institutions in Pennsylvania.
Pennypacker Mills
Pennypacker Mills possesses a lengthy history dating to about 1720 when Hans Jost Hite built the fieldstone house and a gristmill near the Perkiomen Creek, Schwenksville, Montgomery County. Purchased in 1747 by Peter Pennypacker (1710-1770), the house was enlarged and a saw mill and a fulling mill were constructed. The property acquired its name for the three mills.
Peter Pennypacker sold the mills and kept the house which retained the name Pennypacker Mills. In autumn 1777 the house and grounds served as one of General George Washington's headquarters for the Germantown Campaign during the Revolutionary War.
Samuel W. Pennypacker purchased the house from a distant cousin for use as a summer home in 1900 and during his term as governor it was called the "summer capitol." The property surrounding the mansion was landscaped with more than 2,000 native trees by Thomas Meehan and Sons in 1901. The house was extensively renovated and enlarged that year by Philadelphia architect Arthur Howell Brockie, making it the Colonial Revival-style mansion visitors see today. The additions included new parlors, a modern kitchen, laundry room and areas for servants. The servants' spaces – among them a cook's bedroom and workroom and a butler's pantry – have been recently restored and are now featured on tours.
While in office for only one term, Pennypacker made his mark on the Commonwealth which still affects residents. In establishing many of the state departments and agencies which continue to serve the public he created the structure of present-day Pennsylvania government. His decision to establish the Pennsylvania State Police went hand-in-hand with new laws requiring citizens to obtain drivers' licenses, register their vehicles and acquire license plates. His most impressive efforts were in education, child labor and health. He was one of the first political leaders to advocate that children should remain in school instead of working at such an early age. He signed the Commonwealth's first child labor laws specifically aimed at protecting minors who worked in coal mines. Together with laws on food safety and the reporting of illnesses, Pennypacker's initiatives helped save lives.
After he left the governor's office in 1907 Pennypacker Mills became his permanent, year-round residence. The house brims with antiques, objects, books, and mementoes collected by the governor and his family.
In 1981 Montgomery County acquired the house and grounds from the estate of Margaret H. Pennypacker (1906-1980), widow of the governor's son Samuel W. Pennypacker II (1911-1968), whom she married in 1936. Inhabited by eight generations of the family, Pennypacker Mills is one of several historic sites operated by Montgomery County's Division of Parks, Trails and Historic Sites. The National Park Service added the mansion to the National Register of Historic Places in 1976.
Pennsbury Manor, the reconstructed personal country estate and residence of Pennsylvania's first chief executive William Penn (1644-1718), is located in Morrisville, Bucks County, approximately 26 miles northeast of Philadelphia. With sweeping views of the Delaware River, the house is furnished with handsome period furniture, objects and decorative accessories, including a pewter charger (a large shallow platter) once owned by the proprietor. Also on the 43-acre site are a joyner's (woodworker's) shop, icehouse, worker's cottage, smokehouse, necessary house (a 17th-century equivalent of a privy), bake and brew house, kitchen gardens, cemetery and barn.
This year marks the 75th anniversary of the opening of the historic site to visitors. Pennsbury Manor is one of 25 historic sites and museums along the Pennsylvania Trails of History® and is administered by the Pennsylvania Historical and Museum Commission (PHMC) in association with The Pennsbury Society.
Keith House at Graeme Park
Also administered by PHMC, Graeme Park, Horsham, Montgomery County, features the only surviving home of a colonial Pennsylvania governor, the Keith House. In 1723 Sir William Keith (1669-1749), appointed deputy governor of the proprietary colony by Hannah Callowhill Penn, the founder's second wife while he was ill, began building a house on the property which he called Fountain Low. Before constructing the stately residence he had erected a malt house and structures in an industrial complex intended to be used as a distillery. The year the mansion was completed, 1726, was marked by great misfortune for the family. Keith had alienated Hannah Penn who relieved him of his position. His dismissal forced him into bankruptcy and the property was purchased by his son-in-law, physician Thomas Graeme, as a summer estate.
The Keith House is noted for its stylish Georgian period architecture and interior details such as paneling, fireplaces, pediments, window reveals and high ceilings.
Grey Towers
Built as a summer retreat in 1886 for James W. and Mary Eno Pinchot, parents of Gifford Pinchot (1865-1946), who served two nonconsecutive terms as governor, from 1923 to 1927 and from 1931-1935, Grey Towers in Milford, Pike County, is an imposing chateau that looks as if it could have been plucked from the Loire Valley and placed, as if by magic, high in the hills above the picturesque Delaware River in northeastern Pennsylvania. Preeminent 19th-century architect Richard Morris Hunt (1827-1895) – acclaimed in 1986 by New York Times design critic Paul Goldberger as "American architecture's first and in many ways its greatest statesman" – designed the house to reflect the Pinchot family's French heritage. The fieldstone mansion takes its name from conical roofed towers at three of its corners.
With his wife, the flamboyant suffragettist and feminist Cornelia Bryce Pinchot (1881-1960), the governor (who previously served as the first chief of the U.S. Forest Service under two presidents) used Grey Towers to entertain the nation's leading conservationists and members of the General Assembly of Pennsylvania. Cornelia was politically astute and active and waged three unsuccessful bids to represent the state's 15th District in Congress.
Upon the death of his mother, Gifford Bryce Pinchot (1915-1989) donated the estate to the U.S. Forest Service as the family had planned. In 1963 President John F. Kennedy dedicated the Pinchot Institute for Conservation, which plays a role in administering the property, and the National Park Service designated the house a National Historic Landmark.
Grey Towers hosts events and activities throughout the year.
Governor's Residence in Harrisburg
The Governor's Residence in Harrisburg is the fourth official residence to house the Keystone State's first families. Erected on the banks of the Susquehanna River, the 28,600-square foot house containing 32 rooms was designed by Philadelphia architect George M. Ewing Jr. (1917-1993) in the Georgian style. The first floor, accommodating commodious public spaces – state entrance, reception and dining rooms, among others – also serves as galleries in which works of art reflecting the Commonwealth's history and heritage are displayed.
Until the mid-19th century, chief executives and their families were expected to find their own lodgings in the capital city. In 1858, just before leaving office, Gov. James M. Pollock purchased the first governor's house on South Second St. "War Governor" Andrew Gregg Curtin, an intimate and loyal supporter of President Abraham Lincoln, deemed the house too small to conduct the many meetings necessitated by the American Civil War. To remedy the problem, a second official residence, Keystone Hall, 313 North Front St., was acquired in 1864. Keystone Hall was large, awkwardly laid out and drafty, but it intermittently served as home to governors for 96 years until it was demolished in 1960.
In 1941 Gov. Arthur H. James signed legislation authorizing the construction of a new residence, as well as the eventual disposition of Keystone Hall, but the onset of World War II stalled plans for 25 years, until 1966, when ground was broken for the present-day residence. From 1943 to 1955 Govs. Edward Martin, John C. Bell and James H. Duff lived at the State House, a handsome fieldstone farmhouse built for the adjutant general of the Pennsylvania National Guard at Fort Indiantown Gap. Gov. George M. Leader chose to reside at Keystone Hall. He was followed by Gov. David L. Lawrence who, after one year, directed that Keystone Hall be sold at auction and moved his family to the State House. In 1968 Governor and Mrs. Raymond P. Shafer were the first to occupy the residence expressly built for a governor.
The Governor's Residence offers public tours during the months of April, May, June, September and October. Docents conduct special holiday tours in December. Tours are free but reservations are required.
The Snow-Shoe Dance: To Thank the Great Spirit for the First Appearance of Snow by George Catlin (1796-1872). (From Catlin's North American Indian Portfolio, 1845)