The experimental theater company revisits Shakespeare using a 1964 filmed performance of Richard Burton. Here's how to stream it for free.

In Rufi Thorpe's novel, a poor, closeted teenager befriends a wealthy girl, until an act of violence lays their class distinctions bare.

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Little Richard, the flamboyant, piano-pounding showman who injected sheer abandon into rock 'n' roll in its early days, died Saturday. He was 87.

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Little Richard Penniman, a founding father of rock music, died at 87. Before Elvis, the flamboyant singer wowed 1950s teens with his frantic sound.

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Little Richard, whose outrageous showmanship and lightning-fast rhythms intoxicated crowds in the 1950s with hits like 'Tutti Frutti' and 'Long Tall Sally', has died.

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Little Richard, the self-proclaimed “architect of rock ‘n’ roll” whose piercing wail, pounding piano and towering pompadour irrevocably altered popular music while introducing black R&B to white America, died Saturday. He was 87. Pastor Bill Minson, a close friend of Little Richard’s, told The Associated Press that Little Richard died Saturday morning. His son, Danny…

The post Little Richard, Flamboyant Rock ‘N’ Roll Pioneer, Dead at 87 appeared first on The Western Journal.

"Little" Richard Penniman, singer of Tutti Frutti and countless other hits, died Saturday morning. He was 87 years old. Rolling Stone reports that he died of cancer.

Starting with “Tutti Frutti” in 1956, Little Richard cut a series of unstoppable hits – “Long Tall Sally” and “Rip It Up” that same year, “Lucille” in 1957, and “Good Golly Miss Molly” in 1958 – driven by his simple, pumping piano, gospel-influenced vocal exclamations and sexually charged (often gibberish) lyrics. “I heard Little Richard and Jerry Lee Lewis, and that was it,” Elton John told Rolling Stone in 1973. “I didn’t ever want to be anything else. I’m more of a Little Richard stylist than a Jerry Lee Lewis, I think. Jerry Lee is a very intricate piano player and very skillful, but Little Richard is more of a pounder.”

Photo: Anna Bleker (Public Domain) Read the rest

Little Richard, the self-proclaimed "architect of rock 'n' roll" whose piercing wail, pounding piano and towering pompadour irrevocably altered popular music while introducing black R&B to white America, has died Saturday. He was 87.

Junmei Zhang
Feb 1, 2009; 8:215-225
Research

Martin R. Larsen
Jul 1, 2005; 4:873-886
Technology

Bacterial biofilms are cellular communities that produce an adherent matrix. Exopolysaccharides are key structural components of this matrix and are required for the assembly and architecture of biofilms produced by a wide variety of microorganisms. The human bacterial pathogens Escherichia coli and Salmonella enterica produce a biofilm matrix composed primarily of the exopolysaccharide phosphoethanolamine (pEtN) cellulose. Once thought to be composed of only underivatized cellulose, the pEtN modification present in these matrices has been implicated in the overall architecture and integrity of the biofilm. However, an understanding of the mechanism underlying pEtN derivatization of the cellulose exopolysaccharide remains elusive. The bacterial cellulose synthase subunit G (BcsG) is a predicted inner membrane–localized metalloenzyme that has been proposed to catalyze the transfer of the pEtN group from membrane phospholipids to cellulose. Here we present evidence that the C-terminal domain of BcsG from E. coli (EcBcsGΔN) functions as a phosphoethanolamine transferase in vitro with substrate preference for cellulosic materials. Structural characterization of EcBcsGΔN revealed that it belongs to the alkaline phosphatase superfamily, contains a Zn2+ ion at its active center, and is structurally similar to characterized enzymes that confer colistin resistance in Gram-negative bacteria. Informed by our structural studies, we present a functional complementation experiment in E. coli AR3110, indicating that the activity of the BcsG C-terminal domain is essential for integrity of the pellicular biofilm. Furthermore, our results established a similar but distinct active-site architecture and catalytic mechanism shared between BcsG and the colistin resistance enzymes.

The actin cytoskeleton is extremely dynamic and supports diverse cellular functions in many physiological and pathological processes, including tumorigenesis. However, the mechanisms that regulate the actin-related protein 2/3 (ARP2/3) complex and thereby promote actin polymerization and organization in cancer cells are not well-understood. We previously implicated the proline-rich 11 (PRR11) protein in lung cancer development. In this study, using immunofluorescence staining, actin polymerization assays, and siRNA-mediated gene silencing, we uncovered that cytoplasmic PRR11 is involved in F-actin polymerization and organization. We found that dysregulation of PRR11 expression results in F-actin rearrangement and nuclear instability in non-small cell lung cancer cells. Results from molecular mechanistic experiments indicated that PRR11 associates with and recruits the ARP2/3 complex, facilitates F-actin polymerization, and thereby disrupts the F-actin cytoskeleton, leading to abnormal nuclear lamina assembly and chromatin reorganization. Inhibition of the ARP2/3 complex activity abolished irregular F-actin polymerization, lamina assembly, and chromatin reorganization due to PRR11 overexpression. Notably, experiments with truncated PRR11 variants revealed that PRR11 regulates F-actin through different regions. We found that deletion of either the N or C terminus of PRR11 abrogates its effects on F-actin polymerization and nuclear instability and that deletion of amino acid residues 100–184 or 100–200 strongly induces an F-actin structure called the actin comet tail, not observed with WT PRR11. Our findings indicate that cytoplasmic PRR11 plays an essential role in regulating F-actin assembly and nuclear stability by recruiting the ARP2/3 complex in human non-small cell lung carcinoma cells.

Bacterial biofilms are cellular communities that produce an adherent matrix. Exopolysaccharides are key structural components of this matrix and are required for the assembly and architecture of biofilms produced by a wide variety of microorganisms. The human bacterial pathogens Escherichia coli and Salmonella enterica produce a biofilm matrix composed primarily of the exopolysaccharide phosphoethanolamine (pEtN) cellulose. Once thought to be composed of only underivatized cellulose, the pEtN modification present in these matrices has been implicated in the overall architecture and integrity of the biofilm. However, an understanding of the mechanism underlying pEtN derivatization of the cellulose exopolysaccharide remains elusive. The bacterial cellulose synthase subunit G (BcsG) is a predicted inner membrane–localized metalloenzyme that has been proposed to catalyze the transfer of the pEtN group from membrane phospholipids to cellulose. Here we present evidence that the C-terminal domain of BcsG from E. coli (EcBcsGΔN) functions as a phosphoethanolamine transferase in vitro with substrate preference for cellulosic materials. Structural characterization of EcBcsGΔN revealed that it belongs to the alkaline phosphatase superfamily, contains a Zn2+ ion at its active center, and is structurally similar to characterized enzymes that confer colistin resistance in Gram-negative bacteria. Informed by our structural studies, we present a functional complementation experiment in E. coli AR3110, indicating that the activity of the BcsG C-terminal domain is essential for integrity of the pellicular biofilm. Furthermore, our results established a similar but distinct active-site architecture and catalytic mechanism shared between BcsG and the colistin resistance enzymes.

(Molecular Biology and Evolution (Oxford University Press)) In a new paper, Dang Liu, Mark Stoneking and colleagues have analyzed newly generated genome-wide SNP data for the Kinh and 21 additional ethnic groups in Vietnam, encompassing all five major language families in MSEA, along with previously published data from nearby populations and ancient samples.

(US Department of Agriculture - Agricultural Research Service) A new freeze-resistant Trichinella species has been discovered in wolverines by Agricultural Research Service scientists and their colleagues. Trichinella are parasites that cause the disease trichinosis (formally referred to as trichinellosis), which people can get by eating raw or undercooked meat from infected animals.

Qingbo Shu
Apr 1, 2020; 19:672-689
Research

Karl A. T. Makepeace
Apr 1, 2020; 19:624-639
Research