Journal of Biochemistry Advance Access originally published online on April 3, 2007
Journal of Biochemistry 2007 141(5):601-608; doi:10.1093/jb/mvm090
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© 2007 The Japanese Biochemical Society.
JB Minireviews-Genome Decoding Systems |
Phosphorylation of the C-terminal Domain of RNA Polymerase II Plays Central Roles in the Integrated Events of Eucaryotic Gene Expression
Laboratory of Gene Regulation, Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan
*To whom correspondence should be addressed. Tel: +81-76-434-7540, Fax: +81-76-434-5171, E-mail: ohkumay{at}pha.u-toyama.ac.jp
Received December 18, 2006; Accepted March 15, 2007
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Abstract |
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RNA polymerase II (Pol II) is the only polymerase to possess heptapeptide repeats in the C-terminal domain (CTD) of its large subunit. During transcription, CTD phopshorylation occurs and is maintained from initiation to termination. To date, among the three known CTD kinases possessing CDK–cyclin pairs, TFIIH is the only one that forms a preinitiation complex. The Mediator complex plays essential roles in transcription initiation and during the transition from initiation to elongation by transmitting signals from transcriptional activators to Pol II. P-TEFb specifically plays a role in transcription elongation. TFIIH and mediator phosphorylate serine 5 (Ser5) of the CTD heptapeptide repeat sequence, whereas P-TEFb phosphorylates serine 2 (Ser2). Recently, it has become clear that CTD phosphorylation is not only essential for transcription, but also as a platform for RNA processing and chromatin regulation. In this review, we discuss the central role of Pol II phosphorylation in these nuclear events.
Key Words: CTD phosphorylation, mediator, phosphorylated CTD-interacting factor 1 (PCIF1), RNA polymerase II, TFIIH
Abbreviations: CTD, carboxy-terminal domain; Pol II, RNA polymerase II; P-TEFb, positive transcription elongation factor b
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