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CTD - PubMed

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Last Updated: 05 June 2022

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Cooperation between intrinsically disordered and ordered regions of Spt6 regulates nucleosome and Pol II CTD binding, and nucleosome assembly.

"We found that Spt6's acidic N-terminal region of the Pol II CTD and CTD-linker does not restrict the binding of Spt6 not only to the Pol II CTD and Pol II CTD-linker, but also to pre-formed intact nucleosomes and nucleosomal DNA. " Spt6's N-terminal area is associating with the tSH2 domain and Spt6's core, which also controls binding to Pol II and nucleosomes. These results indicate that Spt6's cooperation was greatly enhanced and structured region, as well as the nucleosome and Pol II CTD binding, as well as the nucleosome assembly. ".

Source link: https://doi.org/10.1093/nar/gkac451


Type B CTD Proteins Secreted by the Type IX Secretion System Associate with PorP-like Proteins for Cell Surface Anchorage.

"The Bacteroidetes type IX secretion system consists of at least 20 components that translocate proteins with type A or type B C-terminal domain signals along the outer membrane. " Although type A CTD proteins are tied to the cell surface by covalent attachment to the anionic lipopolysaccharide, it is also unknown how type B CTD proteins are attached to the cell surface. In this research, we discovered a complex consisting of the OM u03b2-barrel protein PorP, the OM-associated periplasmic protein PorP, the OM-associated periplasmic protein PorP, the OM-associated periplasmic protein PorP, and the type B CTD protein PG1035. ".

Source link: https://doi.org/10.3390/ijms23105681


Type B and type A influenza polymerases have evolved distinct binding interfaces to recruit the RNA polymerase II CTD.

"Billy B viruses co-circulate with influenza A viruses during annual influenza epidemics and cause significant morbidity and mortality. " FluPol initiates viral mRNA synthesis and requires a direct correlation of FluPol with the host RNA polymerase II subunit's repetitive C-terminal domain to enable 5'-capped oligomers derived from nascent RNAP II transcripts to prime viral transcription. Here, we present the first high-resolution co-crystal structure of FluPolB bound to a CTD mimicking peptide at a binding site spanning from PA to PB2. "The PB2 627 subdomain, a key determinant of FluPol-host cell interactions and IAV host-range, is involved in CTD-binding for IBVs but not for IAVs, and we also found that FluPolB and FluPolA bind to the host RNAP II independently of the CTD," we discovered.

Source link: https://doi.org/10.1371/journal.ppat.1010328


Oxidative stress induces Ser 2 dephosphorylation of the RNA polymerase II CTD and premature transcription termination.

"The C-terminal domain of the largest subunit of RNA polymerase II consists of YSPTSPS heptapeptide repeats, and the repeater phosphorylation status of the repeats controls multiple transcriptional steps and co-transcriptional events. " Following exposure to H2O2, we discovered that a drastic decrease in phosphorylation of a subset of Ser2 residues occurs quickly but transiently. The diminution of Ser2-P is, at least in part controlled by CK2, but not independent of FCP1 and other common Ser2-phosphatases, according to a new review. And, lastly, the H2O2 treatment had an effect on snRNA 3' processing, although surprisingly the U2 processing was not hindered. Our results show that H2O2 exposure establishes a unique CTD phosphorylation state that rapidly changes transcription to deal with acute oxidative stress, possibly creating a new "emergency brake" mechanism to transiently dampen gene expression. ".

Source link: https://doi.org/10.1080/21541264.2021.2009421

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions

* Please keep in mind that all text is summarized by machine, we do not bear any responsibility, and you should always check original source before taking any actions