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J Biochem. 2007 May;141(5):601-8. Epub 2007 Apr 3.

Phosphorylation of the C-terminal domain of RNA polymerase II plays central roles in the integrated events of eucaryotic gene expression.

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Laboratory of Gene Regulation, Graduate School of Medical and Pharmaceutical Sciences, University of Toyama, 2630 Sugitani, Toyama 930-0194, Japan.


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.

[Indexed for MEDLINE]

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