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- W1448454920 abstract "This chapter discusses (a) the relationship between the state of carboxy-terminal domain (CTD) phosphorylation and the progression of RNAP II through the transcription cycle; (b) the enzymes involved in modulating the state of CTD phosphorylation; and (c) the potential consequences of modifications that occur within the CTD. RNA polymerase (RNAP) II is structurally distinct from both RNAP I that transcribes heavy ribosomal RNA (rRNA) and RNAP III that transcribes a variety of small RNAs, including 5-S rRNA and transfer RNA (tRNA). RNAP II transcribes the greatest diversity of genes, and hence must be able to assemble into preinitiation complexes on a variety of different promoters. The largest subunit of RNAP I1 contains at its c-terminus an unusual domain, consisting of multiple heptapeptide repeats of the consensus sequence, Tyr-Ser-Pro-Thr-Ser-Pro-Ser. This c-terminal domain (CTD) is conserved in evolution and is essential for cell viability. The functions for the CTD is regulated by reversible phosphorylation that include: (a) mediating the interaction of RNAP II, with the preinitiation complex; (b) mediating the release of RNAP I1 from the initiated complex; (c) facilitating the progression of RNAP II through nucleosomes (X); (d) affecting cotranscriptional splicing, by facilitating the association of splicing factors, with the elongation complex; and (e) influencing the specificity of pausing and termination." @default.
- W1448454920 created "2016-06-24" @default.
- W1448454920 creator A5086907855 @default.
- W1448454920 date "1994-01-01" @default.
- W1448454920 modified "2023-10-16" @default.
- W1448454920 title "The Role of Multisite Phosphorylation in the Regulation of RNA Polymerase II Activity" @default.
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- W1448454920 doi "https://doi.org/10.1016/s0079-6603(08)60855-7" @default.
- W1448454920 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/7938548" @default.
- W1448454920 hasPublicationYear "1994" @default.