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School for the Movement of the Technicolor People
Taisha Paggett"s "evereachmore" performance at the Bowtie in the Glendale Narrows - presented/hosted by ClockShop
Photos of Taisha Paggett"s "evereachmore" performance at the Bowtie in the Glendale Narrows - presented/hosted by ClockShop
In collaboration with Ashley Hunt and Kim Zumpfe
Curated by Robert Crouch
Opening reception: Wednesday October 21, 2015 – 7-10PM
Exhibition: October 21-December 6, 2015
Thursday Nov. 12, 2015 – 7PM – Artist Talk with Ashley Hunt, taisha paggett and Kim Zumpfe, moderated by curator, Robert Crouch (Read more)
Saturday, Nov. 14, 2015 – 1-4PM – Movement Workshop and conversation with Ishmael Houston-Jones (Read more)
Tuesday, Nov. 17, 7:30-9:30pm – Public Lecture by the WXPT dance company, with the At Land's Edge platform for visual research
Friday, Nov. 20, 7pm or 8pm – Talk: DJ Lynnee Denise Wednesday, Dec. 2, evening – Movement Workshop: Nic Kay
Saturday, Dec. 5 and Sunday Dec 7:30pm – Closing performance: Meadow (Learn more)
Please check the Saturday class schedule below.
LACE presents The School for the Movement of the Technicolor People, a large-scale installation and performance platform by Los Angeles based artisttaisha paggett. This project, which takes the form of a dance school, is shaped by the question, "what is a Black dance curriculum today?" The installation itself, developed in collaboration with artists Ashley Hunt and Kim Zumpfe, serves as a temporary dance school, performance space and home for dance company, WXPT (We are the Paper, We are the Trees).
The core of The School for the Movement of the Technicolor People is WXPT itself — a temporary, experimental community of queer people of color and allies, dancers and non-dancers alike. WXPT was conceived by paggett in early 2015 to expand upon the language and methods of modern and contemporary dance practices, to shift the ways dancers of color are positioned within the contemporary field, and to explore questions of queer desire, responsibility, migration and historical materials that inhabit our cultural imagination. The company consists of Joy Angela Anderson, Heyward Bracey, Rebecca Bruno, Alfonso Cervera, Erin Christovale, Loren Fenton, Maria Garcia, Kloii "Hummingbird" Hollis, Jas Michelle, Meena Murugesan, taisha paggett, Sebastian Peters-Lazaro, Kristianne Salcines, Ché Ture, Devika Wickremesinghe and Suné Woods.
In May of 2015, paggett organized evereachmore, WXPT's premiere performance created for the Bowtie Project, a partnership between Clockshop and California State Parks to activate an 18-acre post-industrial lot along the LA River. Amidst the recent unfolding of state violence against Black bodies, evereachmore sought to forge new economies of resistance, and new sensations of time, space and togetherness.
Inspired in part by a "school for colored youth" that members of paggett's family founded in early 20th century East Texas, The School for the Movement of the Technicolor People extends the praxis of WXPT into a curriculum and pedagogy. The installation at LACE takes up the form of a school as an artistic and social problem, building the school's curriculum and infrastructure through physical and social sculpture, performance and image, where the roles of artist and viewer, dancing and non-dancing body, art and learning coalesce.
The School for the Movement of the Technicolor People will offer a program of workshops, weekly classes and micro-performances initiated by members of WXPT. The curriculum will be open to anyone, blurring lines between audience and participant, while especially encouraging queer people of color to join. Across the bodies of the company and the members of the public who join the school, the curriculum will build an accumulative performance score in weekly increments, culminating in the performance of a "collective movement choir" at the conclusion of the exhibition.
Each Saturday of the Exhibition: Oct 24 | Oct 31 | Nov 7 | Nov 14 | Nov 21 | Dec 5
12:00pm-12:45pm: opening session
1:00pm-2:20pm: session 1
4:20pm-5:40pm: open rehearsal
Sunday, Nov. 8, 12:00- 3:00pm
Movement for Speculative Quantum Bodies with Anna Martine Whitehead
Anna Martine will lead participants through a movement and discussion-based exploration of blackness and speculative fiction. Beginning with a brief presentation on Quantum Mechanics, Speculative Fiction, and Queer and Trans Black Materiality, the workshop will extend into movement, guided meditation, and contemplative (or a-contemplative) exploration of anatomy. Together, we'll begin working to figure out where our bodies begin and end, and what is beyond our corporeal limits. Participants should come prepared to move and engage; this workshop is about liberation.
Anna Martine is an artist, writer, and performer producing work interrogating identity, space-time, and loss. With an MFA in Social Practice from California College of the Arts, they have shown work in California, New York, Sweden, and throughout the Midwest and the southern states. Martine has also made significant contributions to the work of Keith Hennessy, Jefferson Pinder, taisha paggett, and Julien Previeux. They write a recurring column for Art Practical addressing black creative practice in the modern world, and will be releasing a chapbook through Thread Makes Blanket Press in early 2016. Anna Martine is a recent recipient of Chances Dances' Critical Fierceness grant. annamartine.com
Monday Nov 9: 7PM
Ditch Plains (2013) screening and conversation with Imani Kai Johnson, taisha paggett and Jaye Austin Williams
Facilitated by Erin Christovale
Shot in the East New York section of Brooklyn around the time of Hurricane Sandy, Ditch Plains (HDV, 29 mins) is a dystopian sci-fi street dance film by Loretta Fahrenholz, featuring members of Ringmasters Crew. Like avatars running the levels of an apocalyptic video game, Ringmasters Corey, Jay Donn and Marty McFly hallucinate the city and its networks as a space of terror, mutation and magic. "Flexing," "bone breaking," "pauzing" and "connecting" in nighttime streets, hotel hallways and a posh Park Avenue apartment, the dancers improvise dream-like scenes suggesting digital death-matches, stop-and-frisk situations and catastrophic man-machine interfaces. Meanwhile, documentary shots of Far Rockaway show the city's attempt to manage disaster in real life.
Following the film we will engage in a conversation with scholars Imani Kai Johnson and Jaye Austin Williams and artist taisha paggett around narratives of Black resistance, the intention of Black bodies on screen, socioeconomic privilege in the height of the apocalypse, stop and frisk, and the history of flexing/bone breaking dance style that originated out of Brooklyn. Watch the teaser here.
Please visit wwww.schoolforthemovement.com for more information on events.
The School for the Movement of the Technicolor People began as a conversation between paggett, Rodney McMillian and Cauleen Smith.
taisha paggett's work for the stage, gallery and public space includes individual and collaborative inquiries into the body, agency, and the phenomenology of race and gender. Her projects seek to expand upon the languages and frames of contemporary dance practices, and the limitations of the architecture of conventional dance spaces. Her works include solo and ensemble performance, sculptural installation, and participation as a dancer in the work of other artists and choreographers.
paggett's work has been presented in the 2014 Whitney Biennial, at the Studio Museum in Harlem, Danspace at St Mark's Church (New York); in the Quadruple Consciousness exhibition at Vox Populi (Philadelphia); at Defibrillator (Chicago); and Commonwealth & Council. As a dancer, paggett has worked with artists and projects including Every House Has a Door, Yael Davids, Kelly Nipper, David Roussève/Reality, Meg Wolfe, Vic Marks, Cid Pearlman, Cheng-Chieh Yu, and with Ashley Hunt in their ongoing collaboration, "On Movement, Thought and Politics." A recent recipient of a Headlands artist residency, a UCIRA grant and a MAP Fund grant, paggett is part of the full-time dance faculty at UC Riverside.
Ashley Hunt is interested in how images, objects, maps, writing and performance can engage social ideas and actions, including those of social movements, daily life, the exercise of political power, and the disciplinary boundaries that separate our art worlds from the larger worlds in which they sit. His work looks to structures that allow people to accumulate power, and those which keep others from getting it, while learning from the ways people come to know, contribute to or resist these structures. Rather than seeing art and activism as two exclusive spheres of practice, he approaches them as mutual and complementary — drawing upon the ideas and aesthetics of social movements, cultural theory and art alike, the theorizing and practices of each informing the other.
Recent exhibitions and performances include Cue Art Foundation, Threewalls Gallery in Chicago, The Kitchen in New York, the 2012 Made in L.A. Biennial of the Hammer Museum, Sinopale 4 biennale in Sinop, Turkey, the Museum of Modern Art in New York, the Tate Modern in London, Woodbourne State Correctional Institute in upstate New York, Putnamville Correctional Institution in Indiana, and numerous grassroots and community venues throughout the U.S. Recent writing has appeared in X-TRA Contemporary Art Quarterly (2014), Native Strategies issue 4 (2014), Shifter Magazine #20 (2013). Hunt co-directs the Program in Photography and Media at California Institute of the Arts and is on the faculty of the Visual Arts MFA program at Vermont College of Fine Arts.
Kim Zumpfe is an artist and educator who lives and works in California. She works with images, objects, text, installation, collaborative structures, and exhibitions. In these various media, she is engaged with relationships between the ideological body and subjectivity in locations where multiple bodies develop, displace, produce, and forget to maintain boundaries and relations. Through modes of transformation, she investigates where borders within form disperse – in the body, subjectivity, and politicized space, as a way to interrogate encounters where collapse of identity, intimacy, responsibility, and power structures overlap.
Her work has been exhibited at Culver Center for the Arts Riverside, Visual Arts Center Fullerton, University Art Gallery Irvine, University Art Museum Long Beach, and several public and online sites. She is a member of Emily O, a free-floating artist collective that questions the relationship between individual and collective processes and identity through organizing exhibitions.
Robert Crouch is an artist and curator whose work encompasses sound, performance, and technology. As an artist, he locates his work with the intersection of post-phenomenological listening practices, conceptual sound art, and contemporary electronic music. At it's core, his work can be understood as a conversation between tonality, context, history and subjectivities. Similarly, Crouch's curatorial work focuses on the overlapping disciplines of sound, technology, movement, and performance.
In 2014 he organized the North American premiere of Sphæræ, a large-scale inflatable performance space and public artwork by Dutch artist Cocky Eek. He is currently co-curating Juan Downey: Radiant Nature, a survey of early interactive and performance work of the late Chilean artist as part of the Getty initiative, Pacific Standard Time: LA/LA.
Crouch is the former Associate Director/Curator at LACE, where he curated solo exhibitions with artists Karen Lofgren, Gina Osterloh, Steve Roden, Sean Sullivan, and Margo Victor, and performances with artists including William Basinski, Celer, Lawrence English, Dominick Fernow, and Yann Marussich. He is also the founding partner of VOLUME, a curatorial project that functions as a catalyst for interdisciplinary new media work through exhibitions, performances, events, lectures, and publications, and has worked with a wide range of artists including William Basinski, Nate Boyce, Frank Bretschneider, Richard Chartier, Heather Cassils, Celer, Loren Chasse, William Fowler Collins, Tim Hecker, Isis, France Jobin, Kadet Kuhne, Lucky Dragons, Mamiffer, Carsten Nicolai, Yann Novak, taisha paggett, Steve Roden, Terre Thaemlitz, Julie Tolentino, and Christopher Willits.
Image: Courtesy of Clockshop by Gina Clyne.
The School for the Movement of the Technicolor People is made possible by The MAP Fund, a program of Creative Capital, primarily supported by the Doris Duke Charitable Foundation. Additional funds come from the Andrew W. Mellon Foundation.
This program is sponsored by a grant from the University of California Institute for Research in the Arts.
Development support of School for the Movement of the Technicolor People was given through Show Box L.A.'s Los Angeles Dance & Research Residency Program, which is supported in part by an award from the National Endowment for the Arts.
Photos by Chris Wormald
taisha paggett with WXPT: The School for the Movement of the Technicolor People
Filed Under: Exhibition, Installation, LACE, Performance Tagged With: 2015, Ashley Hunt, dance, Exhibition, installation, Kim Zumpfe, performance, Robert Crouch, Taisha Paggett, taisha paggett with WXPT: The School for the Movement of the Technicolor People, WXPT
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These celebs can't resist a classic game of Bingo, can you?
By Jeremy Edwards
When you think of Bingo, you might not naturally associate the game with glitz, glamour, and showbiz, but it turns out that the humble game is enjoyed by many famous faces, even including some A-listers.
But, of course, it can be tricky for celebrities to get out and enjoy their favorite past-times without being spotted by adoring fans or hounded by paparazzi. Still, on online sites that support Bingo, the online game everyone loves, this classic can be enjoyed from the comfort of their own homes, out of the public eye.
It makes you think – how many of your favorite celebs are playing Bingo right now, as we speak? Whilst we can't give you an answer to that question, we can offer an insight into the famous faces who have been known to enjoy the popular game. Read on to find out more.
Robbie Williams might be asking for permission to entertain us, and it turns out that he gets his own fix of entertainment from playing Bingo. The former Take That member-turned solo artist has had many top hits over the years, but this hasn't led him astray from his love for Bingo. Williams has been reported to enjoy a game or two of online Bingo in his downtime, specifically online tournaments, so there's no telling whether you've had a dauber duel with this star in the past.
Of course, being a successful music artist, Williams hardly needs to play online Bingo for those cash prizes, so he donates any winnings that he makes to charity. Suppose you're a Robbie Williams fan and consider yourself to be particularly observant. In that case, you may have noticed that the musician's music video for 'Feel' was in fact shot outside of a Bingo Hall. So, it's safe to say that he's not at all shy about his love for Bingo.
It turns out that this sports star doesn't just show off his ball skills on the football pitch. He's also partial to a good old-fashioned game of Bingo. The Portuguese footballer first started playing Bingo to help him learn English. But, Ronaldo quickly became hooked on the game and wanted to play for real. And, it turns out that he's now a regular player of the game and has even ventured to Italy, where it is believed the game originated, to play the game as it was intended, in some of the most historical venues.
You'll be happy to hear that the famous female stars aren't letting the men have all the fun playing Bingo since the reality star-turned-author and businesswoman, Katie Price, is a massive fan of the game. It's believed that Price's preferred way to play is on online casino sites, where she can wind down and tuck into some of the exciting games on offer in the comfort of her own home. However, she's also not opposed to attending the land-based casino and has been frequently spotted whipping out her dauber and getting down to some Bingo action at her local Bingo Hall.
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Jeremy Edwards
On Chain Analysis Data Engineer. Lives in sunny Perth, Australia. Investing and writing about Crypto since 2014.

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JVI Classic Spotlights
About JVI
Structure and Assembly
Analysis of the Interaction between the UL11 and UL16 Tegument Proteins of Herpes Simplex Virus
Pei-Chun Yeh, David G. Meckes, Jr., John W. Wills
Pei-Chun Yeh
David G. Meckes
John W. Wills
DOI: 10.1128/JVI.01230-08
The UL11 and UL16 tegument proteins of herpes simplex virus are conserved throughout the herpesvirus family. Previous studies have shown that these proteins interact, perhaps to link UL16-bound nucleocapsids to UL11, which resides on the cytoplasmic face of the trans-Golgi network, where maturation budding occurs. Little is known about the interaction except that it requires the leucine-isoleucine (LI) and acidic cluster motifs in UL11 and that no other viral proteins are involved. In particular, the important question of whether these two proteins bind to each other directly has not been addressed. Accordingly, UL11 and UL16 were expressed in bacteria, and the purified proteins were found to retain the ability to interact in a manner that was dependent upon the LI and acidic cluster. In an attempt to map the UL11-binding site contained in UL16, a large number of deletion mutants were constructed. The first 40 (nonconserved) amino acids were found to be dispensable, but all the other constructs failed to bind UL11 or had poor expression in transfected cells, suggesting that UL16 is very sensitive to alterations and probably lacks a multidomain structure. As an alternative strategy for identifying residues that are important for the interaction, the cysteines of UL16 were investigated, because many of these are highly conserved. Approximately half of the 20 cysteines in UL16 have been shown to be covalently modified by N-ethylmaleimide, and this treatment was found to block the interaction with UL11. Moreover, individual serine replacements of six of the most conserved cysteine residues were made, and four of these disrupted the interaction with UL11 without affecting protein stability. However, the UL11-UL16 interaction does not involve the formation of interspecies disulfide bonds, because binding occurred even when all the cysteines in UL11 were eliminated. Thus, UL16 directly interacts with UL11 and does so in a manner that requires free cysteines.
Herpesviruses have three morphological structures: the icosahedral capsid, which contains the viral DNA; the tegument, a proteinaceous compartment surrounding the capsid; and the lipid envelope embedded with virus-encoded glycoproteins. While the formation of the capsid has been studied in depth (22, 25, 26, 28), the assembly of tegument proteins and final envelopment remain poorly understood. It is thought that some tegument proteins are added to the capsid in the nucleus (7), whereas others are acquired after entering the cytoplasm or traveling to the site of final envelopment at the trans-Golgi network (TGN) (10, 20, 21). Several molecular interactions have been implicated in linking the virus capsid, tegument, and membrane during the envelopment process. Examples include VP22 (tegument)-gD (membrane), VP16 (tegument)-gH (membrane), and UL11 (membrane)-UL16 (tegument/capsid) (20, 21). The focus of this report is the interaction of the UL11 and UL16 tegument proteins of herpes simplex virus (HSV).
UL11, a 96-amino-acid protein, is conserved among all herpesviruses and thought to play a role in the virus budding process at the TGN during nucleocapsid envelopment (2, 12, 17, 29). UL11-null mutants are defective in virus replication and exhibit increased numbers of unenveloped capsids in the nucleus and cytoplasm (2, 6, 12, 17, 29). UL11 is a myristylated protein that accumulates on the cytoplasmic faces of nuclear and Golgi apparatus-derived membranes in infected cells and localizes primarily to the TGN when expressed alone (1, 13, 16, 27). In addition, UL11 has multiple sequences that are required for its proper membrane localization, including cysteines for palmitylation, a leucine-isoleucine (LI) motif, and an acidic cluster (AC) (3, 13). These sequences also regulate the amount of UL11 that is associated with detergent-resistant membranes (3).
UL16 is a 373-amino-acid protein that is also conserved among all herpesviruses (24, 32). It has been identified as a binding partner of UL11 by coimmunoprecipitation, glutathione S-transferase (GST) pull-down, and yeast two-hybrid assays, and the interaction requires the LI and AC motifs of UL11 (14, 31). ACs from other proteins are able to substitute for that of UL11 in trafficking assays, but they disrupt the interaction with UL16, suggesting a high specificity in the recognition (14, 15). More recently, we reported that UL16 dynamically interacts with the capsid (18). In particular, UL16 is stably associated with capsids in the cytoplasm but not those in extracellular virions. Free cysteines appear to play a critical role in this maturation event, because the addition of N-ethylmaleimide (NEM; a chemical that reacts with free cysteines) stabilizes UL16 on the capsids of extracellular virions (18).
We initially proposed that the interaction between UL11 (on the membrane) and UL16 (on the capsid) might provide a bridging function that contributes to the budding process at the TGN (14), but this hypothesis has never been proved. And, while it is clear that no other viral proteins are needed for binding, the crucial question of whether UL11 directly interacts with UL16 has never been addressed. It seemed possible that a cellular protein might be involved, because UL16 recognizes the same information (i.e., the LI and AC motifs) that is used by cellular machinery to traffic UL11 out of detergent-resistant membranes in the absence of other viral proteins (3, 13). That is, UL16 might be a viral homolog of a clathrin adaptor subunit, and if so, it might need to form a complex with particular cellular proteins to function (9, 11). The goals of the experiments described here were to address first whether the interaction is direct or indirect, and second, which part of UL16 is required for UL11 binding. The results prove that the interaction is indeed direct and suggest that the binding mechanism requires several (but not all) of the conserved cysteines within UL16.
Cells, viruses, and antibodies.Vero and human melanoma (A7) cell lines were maintained in Dulbecco's modified Eagle's medium (GIBCO) supplemented with 5% fetal bovine serum (FBS), penicillin (65 μg/ml), and streptomycin (131 μg/ml). The KOS strain of HSV type 1 (HSV-1) (30) was used for these studies, along with recombinants that expressed UL11-green fluorescent protein (GFP) (3) or UL16-cyan fluorescent protein (CFP) (see below). For experiments with pseudorabies virus (PRV), the Becker strain was used. In all cases, infected cells were grown in Dulbecco's modified Eagle's medium supplemented with 2% FBS, 25 mM HEPES buffer, glutamine (0.3 μg/ml), penicillin, and streptomycin.
A His6-specific mouse monoclonal antibody was purchased from Novagen (product number 70796-3). The UL11-specific antibody was produced in rabbits and has been described previously (14). A GFP-specific antibody, produced by Cocalico Biologicals, Inc., was obtained from rabbits injected with purified His6-GFP (3). The anti-His6-GFP-specific serum (diluted 1:3,000) recognizes GFP, CFP, and also the His6 tag, which was fused to the N terminus of GFP and UL16 for purification from Escherichia coli (see Results).
Construction of KOS.UL16-CFP.A derivative of HSV that expresses UL16-CFP was created by homologous recombination. Briefly, the gfp gene of plasmid pCMV.UL16-GFP (14) was replaced with the cfp gene by using flanking BamHI and BsrGI sites. Next, a fragment containing 300 bp downstream of UL16 was PCR amplified from the KOS genome with a forward primer containing a BsrGI site and a reverse primer containing a NotI site, and this fragment was inserted at the 3′ end of the UL16-cfp coding sequence. The resulting plasmid was linearized with EcoRI and transfected into A7 cells, along with purified KOS DNA. Plaques produced by the recombinant virus were identified by fluorescence microscopy, and these were picked for six rounds of purification. Confirmation that the desired virus was obtained was provided by PCR analyses using primers that flank the UL16-cfp coding sequence (yielding a larger product than untagged UL16) and the failure to express wild-type UL16 (as determined both by immunoblotting and radiolabeling-immunoprecipitation assays [data not shown]). Moreover, the recombinant was found to be identical to the wild type with regard to specific infectivity and plaque size, as well as subcellular localization and kinetics of UL16-CFP expression (data not shown).
Construction of BV.UL16-GFP.To create a recombinant baculovirus that expresses UL16-GFP, the chimeric gene was first PCR amplified from pCMV.UL16-GFP (14) using a forward primer containing a BspHI site and a reverse primer containing a NotI site. This fragment was cloned into the pTriEx-1.1 vector (Novagen), which was used to produce the recombinant baculovirus by homologous recombination in insect cells via the BacVector-3000 transfection kit (Novagen). Spodoptera frugiperda cells (Sf21) were maintained in Grace's insect medium supplemented with Yeastolate (Mediatech), lactalbumin hydrolysate (Mediatech), penicillin, streptomycin, and 10% FBS in a humidified incubator at 28°C without CO2. Plaques produced by recombinant baculoviruses were identified by fluorescence microscopy, and these were picked for several rounds of purification. Virus stocks were amplified by infecting suspension cultures of Sf21 cells at a multiplicity of infection (MOI) of 0.2 PFU/cell. Virions were purified from culture medium at 5 to 7 days postinfection and concentrated, and titers were determined as described previously (5, 23).
Expression and purification of His6-tagged proteins.To construct plasmids that encode His6-UL11 (wild-type and LI mutant versions) or His6-UL16, the alleles were cloned into pET-28 (Novagen). The resulting plasmids were transformed into E. coli BL21(DE3) cells (Novagen), and 0.1 mM isopropyl-beta-d-thiogalactopyranoside was added to the cultures to induce protein expression. Proteins were purified by using the His-Bind kit (Novagen). Briefly, approximately 1 g of bacteria was pelleted and resuspended in 10 ml of phosphate-buffered saline (PBS) containing protease inhibitors (P8340; Sigma). The bacteria were lysed by sonication and treatment with 1% Triton X-100 for 30 min at 4°C. After the removal of cell debris and insoluble material by centrifugation at 14,000 × g for 10 min, the lysates were incubated with nickel beads for 30 min. The beads were washed according to the His-Bind protocol, and proteins were eluted in 1 M imidazole and dialyzed overnight against 20 mM Tris-HCl (pH 7.9). Proteins were quantified in standard bicinchoninic acid assays or by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) followed by Coomassie blue staining. On average, the yields of His6-UL11 and His6-UL16 proteins from 1 g of bacteria were 0.2 mg and 0.1 mg, respectively.
GST-fusion constructs.Plasmids encoding wild-type GST-UL11 and mutants lacking the LI, AC, or residues 51 to 96 were described previously (14). To construct a GST-UL11 mutant that lacks the three consecutive cysteines located near the N terminus, the UL11.CCC- allele was PCR amplified from pCMV.UL11-GFP.CCC- (13) and cloned into pGEX-4T-3 (GE Healthcare). The resulting plasmid was subsequently used to make GST-UL11.4C-, which does not contain any cysteines in UL11. This was accomplished by changing the codon for the remaining cysteine in UL11.CCC- (residue 83) to that for alanine (-GCA-) using QuikChange site-directed mutagenesis (Stratagene) according to the manufacturer's protocol. The wild-type UL16 gene was also cloned into pGEX-4T-3 to generate a plasmid that expresses GST-UL16. All GST-fusion proteins were purified from E. coli cells on glutathione beads using the standard methods described by the manufacturer (GE Healthcare).
UL16-GFP mutants.For expression of UL16-GFP derivatives in mammalian cells, deletion mutations and alleles for single amino acid substitutions were created in pCMV.UL16-GFP (14) by either PCR technology or QuikChange site-directed mutagenesis. Codons for cysteines were individually replaced with ones for serine (-AGC-).
GST pull-down assay.GST pull-down assays were done as described previously (14). To analyze the interaction of UL11 with UL16 mutants, pCMV.UL16-GFP derivatives were transfected into A7 cells by means of the calcium phosphate precipitation method. At 20 h posttransfection, the cells were harvested in NP-40 lysis buffer (0.5% NP-40, 150 mM NaCl, 50 mM Tris-HCl [pH 8.0]), and glutathione bead-bound GST-UL11 was added. Proteins bound to the beads were separated by SDS-PAGE, transferred to nitrocellulose membranes, and analyzed by enhanced chemiluminescence-based immunoblotting (GE Healthcare). The same protocol was used to analyze the interaction of GST-UL11 with UL16 produced in Vero cells infected with HSV (wild-type KOS or KOS.UL16-CFP) or insect cells infected with BV.UL16-GFP (all produced in 60-mm plates at an MOI of 1). To detect proteins that were pulled down with GST-UL16 from HSV- or PRV-infected cells, the cells were first labeled with [35S]methionine, as described previously (14). To look for host proteins that might bind to GST-UL11 in complex with UL16-GFP produced in insect cells, SDS-PAGE gels were subjected to zinc staining following the manufacturer's instructions (Bio-Rad).
NEM treatment.To covalently modify free cysteines in UL16, NEM was used at a final concentration of 10 mM (4). For in vitro binding assays, His6-UL16 proteins made in bacteria were purified on nickel beads, as described above. Before they were eluted from beads, His6-UL16 proteins were treated with NEM for 30 min at room temperature. The beads were washed thoroughly, and the proteins were eluted and dialyzed. For baculovirus- or HSV-infected cells, NEM was added to cells that had been resuspended in PBS, and after incubations of 30 min at room temperature, the cells were washed three times with PBS before NP-40 lysis. To examine the effect of NEM on the UL11-UL16 complex, GST pull-down assays were done as before. Then, glutathione bead-bound GST constructs and the associated proteins were treated with NEM for 30 min at room temperature before being analyzed on SDS-PAGE gels.
Search for host proteins that bind UL11 in complex with UL16.It is quite clear that the interaction between UL11 and UL16 does not require any other viral proteins (14, 31); however, it seemed possible that host proteins might be involved in the interaction, because UL16 recognizes the membrane-trafficking signals of UL11 (i.e., UL16 might be a viral homolog of a clathrin adaptor subunit and function in complex with particular cellular proteins). To look for additional binding partners, a recombinant baculovirus was constructed that expressed UL16-GFP at high levels. To determine whether this source of UL16-GFP was still capable of binding specifically to GST-UL11, Sf21 cells were infected with BV.UL16-GFP, and NP-40 lysates were prepared 20 h postinfection. Equivalent amounts of glutathione bead-bound GST or GST-UL11 fusion proteins (Fig. 1A and B) were added to lysate samples, and bound proteins were analyzed by SDS-PAGE and immunoblotting for GFP. Like its mammalian-expressed counterpart (14), baculovirus-expressed UL16-GFP was pulled down by wild-type GST-UL11 and mutant Δ51-96 but not by the AC or LI mutants (Fig. 1C). These results show that no mammalian-specific host factor is necessary for the UL11-UL16 interaction. To look for host factors that might be in the complex, bound proteins were resolved in SDS-PAGE gels and subjected to zinc staining, but no distinct difference was observed between mock- and baculovirus-infected cells (data not shown). This negative result is consistent with the hypothesis that UL11 and UL16 may directly interact.
Baculovirus-expressed UL16-GFP interacts with UL11 via the AC and LI motifs. (A) Diagrams of GST-UL11 constructs. Approximately equal amounts of these constructs as estimated from a Ponceau S-stained gel (B) were mixed with lysates from uninfected (M, mock) or BV.UL16-GFP-infected Sf21 insect cells. The UL11 AC mutant has the approximately same mobility as the Δ51-96 mutant, which has been observed previously (14, 15). (C) Proteins bound to GST constructs were loaded onto SDS-PAGE gels and analyzed by immunoblotting for GFP. When analyzed using densitometry, approximately 40% of the amount of UL16-GFP protein in the lysates (input) was pulled down by GST-UL11.
Binding of purified UL11 and UL16.To further address whether the UL11-UL16 interaction is direct or indirect, these two proteins were made and purified from bacteria to completely eliminate eukaryotic host factors. In the first attempt, His6-tagged UL11 was expressed in E. coli, purified on nickel beads, eluted, and dialyzed. A mutant that lacks the LI motif was also produced for use as a negative control for binding specificity. Various amounts of these His6-UL11 proteins were mixed with glutathione bead-bound GST-UL16 in NP-40 lysis buffer for 2 h at room temperature, conditions identical to those used for the baculovirus experiments. Although no His6-UL11 was pulled down by GST alone, the GST-UL16 construct pulled down only a small amount (less than 1%) of the input His6-UL11, as detected with a His6-specific monoclonal antibody, and very little difference was seen using the LI mutant (Fig. 2A). Because UL16 has many cysteines (18), it seemed likely that GST-UL16 from E. coli might be misfolded to some degree. If so, the misfolding must be specific for the UL11 interaction because GST-UL16 was capable of pulling down virus-specific proteins from HSV- and PRV-infected cell lysates (Fig. 2B), while no prominent proteins were pulled down by GST-UL16 from uninfected cell lysates (data not shown).
Direct interaction assays with UL11 and UL16. (A) The indicated amounts of His6-UL11 proteins were incubated with purified GST only or GST-UL16. Bound proteins were separated by SDS-PAGE and detected by immunoblotting using a monoclonal antibody specific for the His6 tag. WT, wild type. (B) To examine the abilities of purified GST or GST-UL16 to pull down virus-specific proteins, they were incubated with radiolabeled HSV- or PRV-infected cell lysates. Proteins bound were separated by SDS-PAGE, and radiolabeled proteins were detected by autoradiography. Examples of virus-specific proteins pulled down by GST-UL16 are indicated with asterisks. (C and D) Immunoblot analyses were used to show the specificity of rabbit anti-His6-GFP serum for various bacteria-expressed His6-tagged proteins (C) and viral proteins made by wild-type and recombinant HSV strains (D). (E) The indicated amounts of His6-UL16 proteins were incubated with purified GST only or GST-UL11. Bound proteins were separated by SDS-PAGE and detected by immunoblotting. (F and G) Aliquots (1.8 μg) of His6-UL16 protein were incubated with approximately equal amounts of GST-UL11 or mutants (Δ51-96 or LI or AC mutants) as estimated from a Ponceau S-stained gel (F), and bound proteins were analyzed by immunoblotting (G).
In a second attempt to look for direct interactions, the GST and His6 tags were switched. The hope was that His6-UL16 might be better able to fold if it was not linked to GST, which is well known to form a dimer. The switch of tags produced a minor problem in that the His6-specific monoclonal antibody (Novagen) (as used in Fig. 2A) unexpectedly cross-reacted with purified GST-UL11 (data not shown). Fortunately, this problem could be eliminated by using a polyclonal rabbit antibody against His6-GFP. This antibody reacts with His6-GFP, His6-UL11, and His6-UL16 (Fig. 2C), but it does not react with UL11 or UL16 (Fig. 2D, lane 1) unless they are tagged with CFP or GFP (Fig. 2D, lanes 2 and 3, respectively). Using this antiserum in the interaction assay, purified GST-UL11 was readily able to pull down purified His6-UL16 in a dose-dependent manner (Fig. 2E). Importantly, the Δ51-96 mutant could also bind to His6-UL16, but the LI and AC mutants could not (Fig. 2G), even though approximately equal amounts of each of the GST-fusion proteins were used (Fig. 2F). These data prove that UL11 directly interacts with UL16 and that both the acidic cluster and LI motifs are essential for the interaction.
Deletion analysis of UL16.In an attempt to map the UL11-binding site contained in UL16, several N-terminal and C-terminal deletion mutants were constructed in the context of the eukaryotic expression vector, pCMV.UL16-GFP (Fig. 3A), and these were transfected into A7 cells. All mutants were expressed well (Fig. 3B); however, in the GST-UL11 pull-down experiment, only one mutant, NΔ40, was found to retain the ability to bind to UL11 (Fig. 3C). Because the N-terminal 40 amino acids reside in the least-conserved region among UL16 homologs (not shown), it is not surprising that they were found dispensable for UL11 binding. Numerous other truncation and internal deletion mutants were constructed (Fig. 3D), but many of these had no or poor expression (summarized in Fig. 3D), and all those that did express were unable to bind to UL11 (data not shown). These results suggest that UL16 is very sensitive to mutations, at least with regard to the requirements for UL11 binding.
The first 40 amino acids of UL16 are not required for UL11 binding. (A) Diagrams of UL16 wild-type (WT) and N- and C-terminal truncation mutants, which were all constructed as GFP-fusion proteins. (B) Expression levels of indicated constructs in transiently transfected A7 cells. At 20 h posttransfection, cells were harvested in sample buffer, loaded onto SDS-PAGE gels, and analyzed by immunoblotting for GFP. (C) Transfected cells were lysed and incubated with purified GST-UL11 proteins. Bound proteins were analyzed by SDS-PAGE and immunoblotting for GFP. (D) Summary of expression levels of other UL16 mutants.
Sensitivity of the interaction to NEM treatment.As an alternative strategy for identifying residues that are important for the interaction, the cysteines of UL16 were investigated because many of these are highly conserved (32). NEM is a very small (125-Da) membrane-permeable molecule that has long been used to chemically modify free cysteines (8). Recent studies have shown that about half of the 20 cysteines in UL16 can be modified by NEM, and this treatment stabilizes the interaction of the protein with the extracellular capsid (18). To examine the possibility that free cysteines might also be important for UL11 binding, UL16 was treated with NEM and then tested for binding.
Vero cells were infected with a recombinant HSV that expresses UL16-CFP. At 20 h postinfection, infected cells were treated with NEM for 30 min at room temperature, washed, and then lysed in NP-40 buffer to test for binding in GST-UL11 pull-down assays (Fig. 4A and B). A blockage of the UL11-UL16 interaction was observed (Fig. 4B, lanes 1 and 3). Identical results were obtained using wild-type HSV (data not shown). The same blockage was also observed when baculovirus-expressed UL16-GFP was treated with NEM in the GST-UL11 pull-down assay (data not shown). In these assays, the cells were washed thoroughly to remove excess NEM before being lysed, but it was important to consider the possibility that residual NEM might disrupt the interaction. To address this, UL11 and UL16 proteins were allowed to bind prior to the addition of NEM, and the complex was found to be stable (Fig. 4B, lane 2). Hence, it is clear that modification of UL16 with NEM blocks UL11 binding.
UL11 cannot interact with NEM-modified UL16 from infected cell lysates. (A and B) Vero cells were infected with HSV.UL16-CFP at an MOI of 1. At 20 h postinfection, cells were scraped into PBS. One set of cells were treated with NEM for 30 min before detergent lysis. Cell lysates were incubated with approximately equal amounts of glutathione bead-bound GST-UL11 as estimated from a Ponceau S-stained gel (A). Bound proteins were analyzed by SDS-PAGE and immunoblotting (B). For lanes 2 and 3, the addition of NEM was either after (A) or prior (P) to the 2-h incubation. (C and D) GST-UL11 fusion proteins as detected in a Ponceau S-stained gel (C) were mixed with either untreated or NEM-treated HSV.UL16-CFP- infected cell lysates, and bound proteins were analyzed by SDS-PAGE and immunoblotting.
The NEM treatment results raised the possibility that free cysteines in UL11 and UL16 might form irrelevant disulfide bonds when mixed together. To examine this, cysteine mutants of UL11 were constructed. Of the four cysteines in UL11, three are located near the N terminus (residues 11 to 13), and the fourth is located in the dispensable second half of the molecule (residue 83). UL11 mutants lacking three (CCC-) or all four (4C-) of the cysteines were expressed as GST-fusion proteins and purified from bacteria. Both mutants retained the ability to interact with UL16-CFP produced in infected cells (Fig. 4C and D). Identical results were obtained using untagged UL16 expressed by wild-type HSV (data not shown). Moreover, pretreatment of the infected cells with NEM blocked the interaction (Fig. 4C and D, lanes 7 to 9).
The UL11 mutants were also examined for their ability to interact with His6-UL16 purified from bacteria as described for Fig. 2, and as expected, direct binding was observed (Fig. 5B and C). When the His6-UL16 protein was treated with NEM prior to its elution from the nickel beads, a large increase in its mass was observed (Fig. 5A), indicating the presence of multiple free cysteines. As predicted, the modified protein lost its ability to bind UL11 (Fig. 5B and C). Collectively, these results demonstrate that interspecies disulfide bonds are not required for a stable interaction.
NEM modification of UL16 inhibited the in vitro UL11-UL16 interaction. (A) His6-UL16 proteins purified from bacteria were treated with or without NEM and analyzed by immunoblotting. (B and C) Aliquots (1.2 μg) of untreated or NEM-treated His6-UL16 proteins were incubated with approximately equal amounts of GST-UL11 fusion proteins as estimated from a Ponceau S-stained gel (B), and bound proteins were analyzed by immunoblotting (C).
Cysteine substitution mutants of UL16.It would be a daunting task to analyze all 20 of the cysteines in UL16; however, a small subset of these are highly conserved (Fig. 6A). To determine whether any of these are important for the interaction with UL11, six were individually replaced with serine in the context of UL16-GFP. Plasmids encoding the resulting mutants, designated C1S to C6S, were transfected into A7 cells, and each was found to be expressed as well as wild-type UL16-GFP (Fig. 6B). Mutants C1S and C2S retained the ability to interact with GST-UL11, but the other four were completely inactive for binding (Fig. 6C). These results further support the hypothesis that free cysteines (perhaps conserved ones) in UL16 play a critical role in the interaction with UL11 (see below).
Conserved cysteines within UL16 are important for UL11 binding. (A) Alignment of regions in UL16 homologs containing six highly conserved cysteine residues. The residue numbers in this region of HSV-1 are indicated. HCMV, human cytomegalovirus; EHV, equine herpesvirus; HHV, human herpesvirus; EBV, Epstein-Barr virus; VZV, varicella-zoster virus. (B) Expression levels of HSV-1 UL16-GFP wild type (WT) and six cysteine-to-serine substitution mutants (C1S to C6S). Codons for the six cysteines indicated in panel A were individually replaced with codons for serine and constructed into the GFP expression vector. The alleles were transfected into A7 cells, and protein expression was examined by immunoblotting for GFP. (C) GST-UL11 pull-down assays. Transfected cells were lysed with detergent and incubated with glutathione bead-bound GST-UL11. Bound proteins were analyzed by SDS-PAGE and immunoblotting for GFP.
Although the UL11 and UL16 proteins of HSV are conserved among all the herpesviruses, very little is known about their structure and function. Based on the available information, we previously hypothesized that an interaction between these proteins (either directly or indirectly) might provide a bridging function that contributes to the budding process at the TGN (14). The goal of this study was to more precisely define the molecular interaction that was previously predicted to occur (14, 31). When purified from bacteria, the two proteins were found to be capable of interacting directly and in a manner that is dependent upon the acidic cluster and LI motifs of UL11, which were previously shown to have roles in the interaction with UL16 (14, 15). However, the molecular tags used for protein purification were found to be of crucial importance to the success of the experiments, a finding that provides important guidance for future studies. In this regard, it is also important to have learned that UL16 is highly sensitive to deletions throughout its length, and hence, it probably does not have a separate domain that is devoted to binding UL11. This means that elucidation of the residues in UL16 that actually contact UL11 will be difficult. Nevertheless, the mutational analyses described here provide evidence that free cysteines somehow play a role (see below).
Implications for virion maturation.It was previously shown that the interaction of UL16 with capsids changes during egress (18). In particular, UL16 is stably associated with cytoplasmic capsids isolated from NP-40-treated cell lysates, but this interaction is very different in extracellular virions, where disruption with NP-40 under identical conditions releases UL16 from the capsid. More recently, we showed that the natural trigger for the release of UL16 from the capsid occurred upon the attachment of virus to the host cell (19). Free cysteines appear to play a critical role in this release mechanism because the addition of NEM stabilizes UL16 on the capsids of extracellular virions (i.e., it is no longer released from the capsid by NP-40 treatment). Stabilization is also observed when extracellular virions are exposed to low pH (5.0 to 5.5), conditions that protonate free cysteines, making them less reactive (18). However, there are likely to be many proteins in the virion that have free cysteines, and hence, the change in the UL16-capsid association properties seen with NEM treatments could be complex.
In the experiments described here, NEM modification of purified UL16 was found to directly block the interaction with purified UL11, a finding that was further supported by the inability of some (but not all) UL16 cysteine substitution mutants to bind UL11. Based on these observations, we can now hypothesize that the interaction of UL16 with the capsid may be destabilized as a result of binding to UL11 during budding. In other words, when the capsid traverses the cytoplasm and arrives at the TGN, UL16 may engage UL11 and undergo a conformational change, making it sensitive to release by NP-40. Although these ideas are highly speculative, our findings represent the initial glimpses of a molecular mechanism that is present in the tegument.
Possible roles for cysteines in UL16.There are 20 cysteines in UL16, and sequence alignments revealed a cluster in the second half of the protein that is highly conserved (Fig. 6A) (32). The substitution mutants described here reveal that some, but not all, of these residues are important for UL11 binding. While it is possible that these cysteines directly contact UL11, there are several other (perhaps more likely) possibilities for what they do. Some cysteines may be needed merely for the proper folding of the protein, much like any other amino acid in UL16. Other cysteines might serve more complex structural roles, either as participants in disulfide bonds or as components of metal-binding domains (e.g., zinc fingers). It is also possible that UL16 is an enzyme that utilizes one or more free cysteines in its active site. For example, protein disulfide isomerases, which catalyze the formation and breakage of disulfide bonds, generally have a C-X-X-C motif in their active site, and this motif is also found among the conserved residues of UL16 (Fig. 6A). Further complicating the study of this protein is the possibility that all of these roles for cysteines will be found in UL16. Moreover, the role of any particular cysteine may change during virion budding and egress (e.g., particular disulfide bonds may be formed, broken, and rearranged along the way). Hence, much caution is needed when interpreting the results of any cysteine mutants, especially within the far more complicated context of recombinant viruses.
We extend special thanks to our colleagues Nicholas Baird, Jacob Marsh, and Carol Wilson for helpful discussions and encouragement. Additional thanks go to Harriot Isom for providing Sf21 cells and to Richard Heipertz, Jr., and Susan Kocher for their expertise in the construction and growth of the recombinant baculovirus.
This work was supported by NIH grants to J.W.W. (AI071286) and in part by a training grant from the National Cancer Institute (CA60395) for support of D.G.M.
Received 13 June 2008.
↵*Corresponding author. Mailing address: Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, P.O. Box 850, Hershey, PA 17033. Phone: (717) 531-3528. Fax: (717) 531-6522. E-mail: jww4{at}psu.edu
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Pei-Chun Yeh, David G. Meckes Jr., John W. Wills
Journal of Virology Oct 2008, 82 (21) 10693-10700; DOI: 10.1128/JVI.01230-08
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You Are Here: Home → News → Majority of Brits make lifelong friendships at work
Majority of Brits make lifelong friendships at work
Aphrodite Papadatou Friday, January 18, 2019 0 Comment 4Com, Colleagues, employee research, employee survey, friendly workers, romantic relationships, work friends, workplace relationships, Workplace romance
The average full-time worker in the UK clocks 37 hours per week, but just how well do we know the person sat across from us, or those who say "good morning" while making a brew?
New research has looked into Britons attitudes towards their co-workers to reveal just how willing the nation is to create meaningful friendships and relationships with those they spend so much time with day-to-day.
While a quarter (25 per cent) of workers admit to not making lifelong friends with a work colleague, three quarters (75 per cent) have taken their professional relationships to the next level and developed friendships with a co-worker.
When asked why they've never made meaningful friendships with their co-workers, the top five reasons were: They're there to a job, not make friends (39 per cent); They have nothing in common with the people they work with (25per cent); They don't want to be reminded/speak about work when outside of work (18 per cent); It can cause a lot of drama (16 per cent); They already have a lot of friends outside of work and don't need anymore (13 per cent)
For the 75 per cent who have broken the professional barrier however, the study investigated if the friendship makes them more productive at work. The top three reasons were: It makes them enjoy their job more (72 per cent); They can always rely on them if anything goes wrong (38 per cent); It makes getting out of bed in the morning much easier (36 per cent)
The research also explored the reasons we might choose to merge work friends with other friendship groups or why we would choose to keep the two worlds separate.
Two fifths (40 per cent) said they'd be happy to combine the two due to both parties being easy to get along with. For one in five (21 per cent) it's an easy merge thanks to their similar interests, and one in seven (15 per cent) choose to bring the two together for their own convenience.
Of those who always keep their friendship groups apart, 5 per cent are worried one will feel left out, 5 per cent think their interests are too different and 13 per cent say they prefer to keep their professional and personal lives separate.
But, could this need for separating the two elements of our lives be down to the fact that nearly half (41 per cent) of UK workers who have made lifelong friendships with co-workers, have a colleague they refer to as their "work wife" or "work husband"?
The top three reasons for this "work-spouse" relationship are: I trust them with my secrets (17 per cent); They make me smile and laugh (13per cent); I have a lot in common with them (12 per cent), we argue like husband and wife (12 per cent)
With a large majority of UK workers having made meaningful relationships with co-workers, Dr Elena Touroni, of The Chelsea Psychology Clinic comments on the development of these relationships,
It's easy to feel like you're going through a connecting experience with your colleagues when you're constantly problem solving and finding solutions and it's an effective way to boost productivity. When we develop friendships, there is more positive energy and we build a support system making it an environment you enjoy being in and therefore are more willing to get your work done.
When it comes to those naming each other their "work wife" or "work husband", these kinds of relationships should be managed with caution. There is a very fine line that can easily be crossed when there's vulnerability in one's existing relationship with their partner.
Those who have experienced a shift to friendship or relationship with a co-worker describe how it happened for them:
Liv, a PR Account Director from London, and Chantelle, Owner and Founder of Oriani & Co, a luxury fashion brand:
Liv says,
I met Chantelle on her first day of work at Weber Shandwick. My boyfriend had broken up with me the day before, completely out of the blue, and the last thing I wanted to do was take the new girl out for lunch and make small talk! Chantelle and I immediately hit it off, and in the space of an hour, we both knew each other's life stories and she went on to help me through a really difficult time.
Since that day, we spent every breakfast and lunch together for over two years. Chantelle has now left Weber Shandwick to pursue her own business, but we still speak every day and meet up as much as possible. Work of course, just isn't the same without her.
Stefanie Hopkins, Brighouse, West Yorkshire, founder and managing director of Faith PR:
I met Carl in 2004 when I worked as an account manager at the marketing agency he owned in Leeds. I didn't have much to do with him on a daily basis until I was put in charge of organising the company's 21st birthday bash and had to work more closely with him.
Soon after, he threw a party at his house for his 40th birthday and invited us all. On the way home, I texted a colleague to say how much I liked Carl but accidentally sent it to him. When he replied: "What are you talking about?" I was mortified and confessed. He didn't reply, and I was in a huge panic that my job would be on the line.
To my surprise, a few days later he invited me to have lunch with him and then for dinner at his house. For several months we kept things quiet but eventually our relationship was outed when a colleague spotted me getting out of Carl's car one morning. Some colleagues treated me differently, others were shocked by the 13 years age difference, but thankfully friends were supportive. We got married in July 2007 and have two children together.
Commenting on the research, Mark Pearcy, Head of Marketing at 4Com, said,
We spend a lot of time with our colleagues, more so than with our other friends and family, so it's nice to see we're building strong and meaningful relationships with these people. It's also lovely to hear so many of us are merging friends with our work friends and that these relationships are making people more productive while at work.
*Research by 4Com
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Barbra Streisand's Masterpiece Yentl Finally on DVD
Barbra Streisand's Yentl is my favorite movie ever. It has just been released for the first time on DVD as a two-disc "Director's Extended Edition."
When I am asked about my favorite movie and I give the answer of Yentl, more often than not people react with a giggle and "Oh, of course Yentl is your favorite movie. Gays love Barbra Streisand."
Heaven forbid there might be some personal resonance or artistic merit involved!
The one follow-up question I am never asked is, interestingly enough, the same question the character of Yentl asks throughout Streisand's film.
To hear my family tell it, I was interested in Barbra Streisand from the time I was three and learned to put records on my parents' turntable. For birthdays and holidays, everyone knew to get me whatever Barbra Streisand record I didn't have. If a Streisand movie was on TV past my bedtime, I had to be allowed to stay up and watch it.
At a certain point, my interest in Streisand became stronger because I'd read she was teased as a child. As I was teased pretty badly throughout grammar school, this spoke to me. I thought, "If she can be teased and become who she is, then so can I."
I was 13 years old in November of 1983 when the ABC News program 20/20 was going to devote an entire hour to Streisand and Yentl, which would be released nationally in December.
In today's overstuffed entertainment marketplace, such a program may not sound all that special or unique. However, in 1983, with only three networks and a couple of local stations, this was a big deal. At that time, Streisand was unequivocally the world's biggest and indeed, greatest, star. She rarely gave interviews.
Although I had the albums and seen the movies on TV, I'd never heard the woman speak as herself. This 20/20 special was an Event and Exciting, both with a capital E.
20/20 subtitled the special, "Papa, Watch Me Fly" as a great deal of Streisand's reasoning and drive to get Yentl made stems from the loss of her father when she was 15 months old. She never knew him.
During the interview, Streisand spoke of her brother taking her to the cemetery where her father is buried. She had never been there. Her brother snapped a photo as she put her arm around her father's tombstone and she considers it the only picture she has with her father. None were taken of the two of them while he was alive.
Streisand also related that in the Issac Bashevis Singer short story on which Yentl is based, Yentl has a dead brother named Anshel (actually, she was incorrect about the relation; in Singer's story, Anshel is referred to as a late uncle).
The character of Yentl disguises herself as a boy in order to study Talmud, which at the time of the story, was forbidden to women. As a boy, she takes the name Anshel.
When the photo with her father's tombstone was developed, her assistant noticed something. "Barbra," he said, "look at the name on the tombstone next to your father's." The man's name was Anchel. Although the spelling was off by one letter, Streisand took this as a "sign." She decided to muster the nerve not only to get the film made and star in it, but direct as well. The latter is something no one in Hollywood wanted her to do.
Videocassette recorders were just becoming vogue when this interview aired, so I re-watched the program several times over the next few weeks with many members of my family. One viewing was with my grandparents. When Streisand told the story of the name Anshel and what a rare name it is, my paternal grandmother turned to me and said, "You know, your father's middle name is Anshel."
This information gave me a rather profound "connection" to Streisand and Yentl. For years, people who knew I was a big fan would ask, "What would you say if you ever met Barbra Streisand?"
My answer was always, "I'd tell her my father's middle name is Anshel."
On December 10th, 1983, I saw Yentl for the first time. What I recall most is how my identification with the character of Yentl was solidified the moment we see her in disguise. She hails down a carriage in order to get a ride to the next town. The horse-driver takes Yentl's money, then charges off without letting her get in the wagon.
Later, Yentl (she has not yet assumed the name of Anshel) enters an inn filled with Yeshiva boys. A bully challenges Yentl to arm wrestling; money is involved and Yentl loses twice. Another man, Avigdor (Mandy Patinkin) sees what is happening and insists the bully give Yentl her money back.
Both of these moments echoed the times kids would steal my lunch money or challenge me to a fight. When Avigdor came to Yentl's rescue, I wished I'd had an Avigdor of my own to stick up for me like that.
Later, as Avigdor and Anshel become study partners and good friends, there is a scene where the two are walking by a river arguing Talmud. Avigdor becomes playful with Anshel, chasing him, rough-housing and eventually tackling Anshel to the ground. Amidst laughter there is a moment where the two stop and look at each other.
Of course, the audience knows Anshel is really a woman played by Barbra Streisand. Certainly Avigdor is responding to Anshel/Yentl's feminine energy. However, Avigdor does not know Anshel is a woman, so the homoerotic implications are quite charged.
Of course, Yentl falls in love with Avigdor, and by the time she sings (in voiceover) "Will Someone Ever Look At Me That Way?," I was completely in sync with Yentl's feelings. The brilliant Alan and Marilyn Bergman provided these lyrics:
"Do my eyes forget themselves
and do I ever look at him and smile in such a way that what I'm feeling shows?
Sometimes I have the feeling everybody knows."
At that time, I did not have words for my feelings, but I knew I was more interested in men than women. As a young boy realizing my emotional romantic leanings, those Bergman lyrics were instantly intrinsic.
I was constantly afraid my feelings were obvious and that I would be punished for them. I thought that if I were ever to have a friend like Avigdor, I would find myself in the same position as Anshel/Yentl. I would have to hide my affection, and ultimately hide who I really was.
My second viewing of Yentl was accidental, yet an even more powerful memory. Another kid named Peter and I were dropped off at the Lincoln Village Theater in Chicago by Peter's father, who got us in to see a Rated R "T & A" flick called Hot Dog: The Movie. When Peter's father couldn't come pick us up right away after Hot Dog ended, Peter suggested we sneak in and see Yentl. Of course, I wasn't going to object!
We sat in the back of the theater and Peter kept cracking jokes. He had become quite loud about it, and I halfheartedly went along to "be cool." A man approached us and basically threatened us into piping down. In my head I was shouting, "It's not me, it's him! I love this movie!"
At the finale, when Yentl's disguise has ended and Streisand as Yentl performs the soaring "A Piece of Sky," I began to weep. I know this second viewing was when my soul's resonance with Yentl hit me in one fell swoop.
It was a combination of so many things. There was my empathy towards Barbra Streisand in terms of love for a father she never knew (the dedication at the end credits made me cry harder). There was the fact that the name she takes as a boy is a name my father shares. Earlier that year, I had my bar-mitzvah. It was a time when my identification as a Jew was at its height. Watching a film that treated students of Judaism with such love and affection could not have occurred at a better time.
Beyond that, there was my reaction to the tremendously moving and beautiful music by Michel Legrand and certainly, but not least, the allegorical quality of the story compared to my own inner life experience. I had a secret. Yentl did too. She found a way to be free of that secret. Would I?
For weeks that followed, the razzing I already endured at school was heightened because Peter told everyone, "Paul cried at the end of Yentl."
Over the years, my affection for Yentl only grew stronger. When it was shown on cable, I not only recorded it on videocassette, but stuck a small audio recorder up to the television speaker so I could listen to the movie at night when I couldn't watch TV without waking up my family. As a result, I know the sound of Yentl inside and out.
My early teenaged emotional reaction to Yentl became enhanced by my burgeoning study of film and more sophisticated understanding of how a movie gets made. When I would watch Yentl, I found myself studying the technical aspects intently.
I would marvel at how what the camera captured was so expertly timed to the music (in particular during the first occurrence of "No Wonder" and "Will Someone Ever Look At Me That Way?"). Terry Rawlings' editing and Ms. Streisand's staging is particularly exciting during the "Tomorrow Night" sequence. David Watkin's lighting choices are fascinating. I love that when books are opened, light bounces off of the pages, illuminating both the words and the character reading.
I found symbolism within Streisand's choices. One aspect she has confirmed before (and again for this DVD release) is the notion that each time the character of Yentl makes a significant step in her journey she "crosses over" a body of water.
One she has not confirmed is my notion that that the final sequence, "A Piece of Sky" was designed to be representative of Yentl's entire journey.
At the opening of the "A Piece of Sky," Yentl is off to "a place where she hears things are different." She is at the rear of a boat, alone and singing aloud, asking questions of her father. This section can be equated with the opening of the film until Yentl's father dies.
At the song's bridge, Yentl walks through the boat's interior. Streisand ceases to lip sync but her vocal continues, which is consistent with Streisand's choice to have the character of Yentl "sing out" only when she was alone. This "silent walk" correlates to the entire masquerade of Anshel, and Yentl's inability to reveal the truth to those around her.
Streisand discards the choice of interior monologue when Yentl is around others in the next shot, as Yentl emerges from darkness. For all these years, I thought Yentl went from one end of the boat to the other, but one of the extras on the new DVD makes it clear she is going from the lower deck to the upper deck. I love this because, spiritually speaking, it indicates Yentl has gone from a lower level to a higher level.
Yentl sings out in front of all the other emigres to America. The "secret" of Anshel is over. Yentl has told the truth and can express herself fully to the world. She is no longer concerned with hiding; everyone on that boat and in the heavens can hear her. She has come from darkness into light and air.
Here, Yentl stops questioning her father. ("Papa...I CAN hear you; Papa...I CAN see you; Papa....I CAN feel you....Papa....watch me FLY!). The mood is triumphant. There is no doubt she will still ask questions, but she no longer needs to question where her father is concerned.
Barbra Streisand's talent has proven itself to be limitless for coming up on 50 years. Nevertheless, I consider Yentl to be her ultimate artistic statement. Everything that she is capable of doing (directing, producing, writing, acting, singing, etc.) is in this film. Her artistry and intelligence are firing on all cylinders.
There was no Streisand project like Yentl before it (Funny Girl may come close) and she hasn't done anything like it since. Her follow-up films have their merits, but the closest she has come to something equally extraordinary and moving has only occurred when she revived music from Yentl during stunning sequences for her 1994 and 2000 concert tours. These sequences consistently garnered Streisand her loudest ovations, rendering unquestionable that no project has stirred Streisand's fans on the level of Yentl.
That is why I always found it strange that Yentl had not been released on DVD even in a bare-bones edition. The demand for it in her fan circle has been enormous.
As Yentl is the final film of Streisand's to be released on DVD, the best was saved for last. More care, effort and time has been taken in preparing this release by comparison to any other Streisand film currently available in the format and deservedly so.
Disc One features an option to watch the theatrical or extended cut of the movie, the latter of which reincorporates three scenes pulled from Streisand's archive. In the extended version, the first "new" scene does not appear until approximately an hour and a half has passed.
What is most interesting about two of the three reincorporated scenes are that neither features the character of Yentl. Until now, the only scene where Yentl was not an onscreen presence was towards the end, where we see Avigdor and Hadass reading a letter from her. It is interesting that Streisand chose to put these scenes back in, as it shifts the movie from being completely Yentl's perspective (albeit briefly).
In another section on Disc One, we are shown more cut moments. There are two other scenes I felt were actually more worthy of being reincorporated. One is where Anshel offers to sew the torn lapel of Avigdor's jacket (symbolizing the end of Avigdor's mourning over his dead brother). The second is where Yentl (as Anshel) is at school and distracted by her sadness for Avigdor, whose engagement to Hadass has just been broken.
Streisand's feature-length commentary with co-producer Rusty Lemorande is, for the most part, quite technical and puts great emphasis on Streisand's relationship with her crew. David Watkin's photography is commented upon the most and it is fascinating to learn how much of the film was shot with entirely natural light. A minor disappointment is that Streisand does not say much about working with her actors.
Disc Two features a most fascinating behind-the-scenes look called "Rehearsal Process," which allows Streisand fans and film students alike into her creative world. Five musical sequences from the film are featured in comparisons from rehearsal to final film, but the most interesting are those for "Where Is It Written?" and "Tomorrow Night."
The former is shot on black-and-white film and the latter with an early model home video camera. In both it is apparent Streisand had perfected the blocking and fluidity of the camera moves before she started actual production. The similarities to the final film are so close it is almost like having an alternate version.
It is particularly wonderful to see her singing and acting "Where Is It Written?" live on set with nothing but a piano.
Of course, the best part of this DVD is that whether the original cut or the extended cut we can watch the film in a crisp, color-corrected transfer that is just dynamite.
It's an oft told tale that Streisand was robbed of recognition by the Motion Picture Academy at the 1984 Oscars. From my vantage point, it's the biggest and most glaring snub in Oscar history. It is a shame that politics, and perhaps sexism, got in the way of the film (and Streisand personally) being recognized in more categories.
I agree with Roger Ebert who said (in 1987), "It seems that Streisand only received the grudging admiration of the industry and after years of [implying] that she knew more than the directors she was working for, she proved with this movie that maybe she did!"
One of the scandalously few Oscar nominations Yentl received was for Amy Irving's performance as Hadass. As I watched the DVD, I realized that every time I have watched the scene where Hadass tries to seduce Anshel, I have never paid attention to what Streisand was doing. Ms. Irving may be one of the few examples of an actress who stole a scene from Barbra Streisand. Her Oscar nomination was deserved.
Some have been critical of Streisand's performance as Anshel, and feel she is not very believable as a boy. I have always disagreed. She makes very specific acting choices when she is "Yentl" as opposed to "Anshel." The timbre of her voice changes; so does her body language. There may be a few moments here or there where lines get blurred, but overall I think Streisand as a very boyish young man is quite effective.
Yentl has it all: a great love story, moments of sweet comedy, moments of moving drama (Yentl's reveal to Avigdor is particularly powerful). It also boasts gorgeous music, sumptuous art direction and cinematography....
Above all, there is Barbra Streisand's heart, soul and vision pouring out through committed acting, beautiful singing and focused, flawless direction. It is her masterpiece, bar none.
By the way, in 2003, I wrote a letter to The Oprah Winfrey Show when I learned Streisand was going to appear.
That letter enabled me to speak with Barbra Streisand on camera and tell her....
"My father's middle name is Anshel."
Nothing's Impossible!
For more information on Barbra Streisand's incredible career, and more on Yentl, please visit this website.
You can purchase Yentl: Director's Extended Edition via Amazon.com at this link:
Oprah Winfrey Mandy Patinkin The Oprah Winfrey Show Roger Ebert Yentl


text:
Carolyn Persick Vicknair
Carolyn was called to her Heavenly Home on Tuesday, November 3, 2020 at the age of 75. She was a lifelong resident of Livingston, LA. Carolyn was a faithful member of Pine Grove Baptist Church. Her biggest joy in life was working in her yard or being on her lawn mower. Carolyn also enjoyed going camping and fishing. If you could not find her doing one of these, she would be found behind a big platter of boiled crabs. Carolyn adored cooking and making candy for her friends and family. She never met a stranger and genuinely loved everyone. Carolyn was a remarkable woman who will be deeply missed. Carolyn is survived by her husband of 59 years, Norman F. Vicknair; children, Stacey Beregi (Jimmy), Todd Vicknair (Ann), and Pennie LaCombe (Rick); sister, Alice Yuhasz (Richard); grandchildren, Mitchel Vicknair and Carly LaCombe. Carolyn is preceded in death by parents, Alton and Alberta Persick; and brother, Alton Persick Jr. The family wants to extend a huge "Thank You" to the Heart of Hospice, Pine Grove church family, Marilyn, Ms.B, Betty Boo, and Roslan for all the support and love they have given to their family. In lieu of flowers, donations may be made to Pine Grove Baptist Church Caregiver's Fund in honor of Mrs. Carolyn. Relatives and friends are invited to attend the visitation at Pine Grove Baptist Church in Livingston, La. on Friday, November 6, 2020 from 10:00 a.m. until the funeral service at 12:00 p.m. Bro. Paul Taylor will officiate and interment will follow in Pine Grove Baptist Church Cemetery.
Carolyn was called to her Heavenly Home on Tuesday, November 3, 2020 at the age of 75. She was a lifelong resident of Livingston, LA. Carolyn was a faithful member of Pine Grove Baptist Church. Her biggest joy in life was working in her yard... View Obituary & Service Information
The family of Carolyn Persick Vicknair created this Life Tributes page to make it easy to share your memories.
Carolyn was called to her Heavenly Home on Tuesday, November...
Send flowers to the Vicknair family.


text:
package vreplication

import (
	"io"
	"sync"
	"time"

	"golang.org/x/net/context"

	binlogdatapb "vitess.io/vitess/go/vt/proto/binlogdata"
)

type relayLog struct {
	ctx      context.Context
	maxItems int
	maxSize  int

	// mu controls all variables below and is shared by canAccept and hasItems.
	// Broadcasting must be done while holding mu. This is mainly necessary because both
	// conditions depend on ctx.Done(), which can change state asynchronously.
	mu       sync.Mutex
	curSize  int
	items    [][]*binlogdatapb.VEvent
	timedout bool
	err      error
	// canAccept is true if: curSize<=maxSize, len(items)<maxItems, and ctx is not Done.
	canAccept sync.Cond
	// hasItems is true if len(items)>0, ctx is not Done, and interuptFetch is false.
	hasItems sync.Cond
}

func newRelayLog(ctx context.Context, maxItems, maxSize int) *relayLog {
	rl := &relayLog{
		ctx:      ctx,
		maxItems: maxItems,
		maxSize:  maxSize,
	}
	rl.canAccept.L = &rl.mu
	rl.hasItems.L = &rl.mu

	// Any time context is done, wake up all waiters to make them exit.
	go func() {
		<-ctx.Done()
		rl.mu.Lock()
		defer rl.mu.Unlock()
		rl.canAccept.Broadcast()
		rl.hasItems.Broadcast()
	}()
	return rl
}

func (rl *relayLog) Send(events []*binlogdatapb.VEvent) error {
	rl.mu.Lock()
	defer rl.mu.Unlock()

	if err := rl.checkDone(); err != nil {
		return err
	}
	for rl.curSize > rl.maxSize || len(rl.items) >= rl.maxItems {
		rl.canAccept.Wait()
		if err := rl.checkDone(); err != nil {
			return err
		}
	}
	rl.items = append(rl.items, events)
	rl.curSize += eventsSize(events)
	rl.hasItems.Broadcast()
	return nil
}

func (rl *relayLog) Fetch() ([][]*binlogdatapb.VEvent, error) {
	rl.mu.Lock()
	defer rl.mu.Unlock()

	if err := rl.checkDone(); err != nil {
		return nil, err
	}
	cancelTimer := rl.startTimer()
	defer cancelTimer()
	for len(rl.items) == 0 && !rl.timedout {
		rl.hasItems.Wait()
		if err := rl.checkDone(); err != nil {
			return nil, err
		}
	}
	rl.timedout = false
	items := rl.items
	rl.items = nil
	rl.curSize = 0
	rl.canAccept.Broadcast()
	return items, nil
}

func (rl *relayLog) checkDone() error {
	select {
	case <-rl.ctx.Done():
		return io.EOF
	default:
	}
	return nil
}

func (rl *relayLog) startTimer() (cancel func()) {
	timer := time.NewTimer(idleTimeout)
	timerDone := make(chan struct{})
	go func() {
		select {
		case <-timer.C:
			rl.mu.Lock()
			defer rl.mu.Unlock()
			rl.timedout = true
			rl.hasItems.Broadcast()
		case <-timerDone:
		}
	}()
	return func() {
		timer.Stop()
		close(timerDone)
	}
}

func eventsSize(events []*binlogdatapb.VEvent) int {
	size := 0
	for _, event := range events {
		if event.Type != binlogdatapb.VEventType_ROW {
			continue
		}
		for _, rowChange := range event.RowEvent.RowChanges {
			if rowChange.Before != nil {
				size += len(rowChange.Before.Values)
			}
			if rowChange.After != nil {
				size += len(rowChange.After.Values)
			}
		}
	}
	return size
}

redpajama_set_name: RedPajamaGithub


The Mayser Pieter Panama Straw Hat is a cool and comfortable downbrim hat made from genuine panama straw. This panama features a 4" crown with open weave design, 2 1/2" brim on the sides and 2 3/4" front and back, leather hatband, cloth sweatband, and sewn logo pin. Adhesive reinforcement at the crown protects the straw from cracking. Mayser is a premier German hatmaker that we are pleased to offer to our customers. Designed in Germany, hand-woven in Ecuador, finished in Slovakia.


text:
Beyond Brock
Crime/Emergencies
Municipal Bulletins
Police searching for missing man from Orillia
UPDATE: The man has been safely located.
Police are looking for a bit of help from the public to track down a missing man from Orillia.
Tyson Baumgarten, 33, was last seen between 4:30 and 6:30 p.m. on Thursday (July 9) in the area of Colborne Street and Dufferin Street in Orillia.
He is described as 6'3" in heith, with brown, shaggy hair. He was last seen wearing a plaid shirt and black pants, as well as glasses.
Anyone with information on his whereabouts is asked to call the OPP at 1-888-310-1122/
Durham Regional Police chief retiring after 30-year career
Non-medical masks, face coverings now mandatory within most public indoor spaces in Durham
Tragedy averted after kids go through ice in Scugog
Human remains discovered near Lake Ontario in Oshawa
Few new details released by SIU in death of one-year-old boy
DRPS urging residents, businesses to adhere to new lockdown rules
Whitby homeowner facing fine after alleged gathering at outdoor rink
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