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RNA polymerase II C-terminal heptarepeat domain Ser-7 phosphorylation is established in a mediator-dependent fashion.
J. Biol. Chem. 285, 188-196 (2010)
The largest subunit of RNA polymerase II (RNAPII) C-terminal heptarepeat domain (CTD) is subject to phosphorylation during initiation and elongation of transcription by RNA polymerase II. Here we study the molecular mechanisms leading to phosphorylation of Ser-7 in the human enzyme. Ser-7 becomes phosphorylated before initiation of transcription at promoter regions. We identify cyclin-dependent kinase 7 (CDK7) as one responsible kinase. Phosphorylation of both Ser-5 and Ser-7 is fully dependent on the cofactor complex Mediator. A subform of Mediator associated with an active RNAPII is critical for preinitiation complex formation and CTD phosphorylation. The Mediator-RNAPII complex independently recruits TFIIB and CDK7 to core promoter regions. CDK7 phosphorylates Ser-7 selectively in the context of an intact preinitiation complex. CDK7 is not the only kinase that can modify Ser-7 of the CTD. ChIP experiments with chemical inhibitors provide evidence that other yet to be identified kinases further phosphorylate Ser-7 in coding regions.
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Publication type Article: Journal article
Document type Scientific Article
Keywords Gene/Regulation Gene/Transcription; Phosphorylation/Enzymes; Phosphorylation/Kinases/Serine-Threonine; Phosphorylation/Serine/Threonine Transcription; Transcription/Coactivators; Transcription/RNA Polymerase II
ISSN (print) / ISBN 0021-9258
Quellenangaben Volume: 285, Issue: 1, Pages: 188-196
Publisher American Society for Biochemistry and Molecular Biology
Reviewing status Peer reviewed