Journal of Biochemistry Advance Access published online on April 3, 2007
Journal of Biochemistry, doi:10.1093/jb/mvm090
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© 2007 The Japanese Biochemical Society
JB Minireview |
Phosphorylation of the C-terminal Domain of RNA Polymerase II Plays Central Roles in the Integrated Events of Eukaryotic 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: Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan, Phone: +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
| Abstract |
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RNA polymerase II (Pol II) is the only polymerase to among species which possesses heptapeptide repeats inat thethe C-terminal domain (CTD) of itsthe largest subunit. During During transcription, CTD phopshorylation occurs and is maintained from initiation to termination`ination. To date, among the tTthree known CTD kinases possessingcontaining CDK-cyclin pairs, are known. Among those, TFIIH is the only one CTD kinase that formsforming a preinitiation complex. The Mediator complex plays essential roles inat transcription initiation and during the the transition from initiation toto elongation by transmittingmediating signals from transcriptional activators to Pol II. P-TEFb specifically plays a role inat 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 becomebecame clearer that CTD phospshorylation is not only essential for transcription but also as simultaneously gives a platform for RNA processing and as well as chromatin regulation. In this review we discuss the central role of Pol II phosphorylation in the these nuclear eventss.
Key Words: RNA polymerase II, CTD phosphorylation, TFIIH, Mediator, phosphorylated CTD-interacting factor 1 (PCIF1)
+ Present e-mail address: yh620{at}pha.u-toyama.ac.jp
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