Dynamic phosphorylation patterns of RNA polymerase II CTD during transcription

Martin Heidemann, Corinna Hintermair, Kirsten Voß, Dirk Eick

Research output: Contribution to journalReview articlepeer-review

206 Scopus citations

Abstract

The eukaryotic RNA polymerase II (RNAPII) catalyzes the transcription of all protein encoding genes and is also responsible for the generation of small regulatory RNAs. RNAPII has evolved a unique domain composed of heptapeptide repeats with the consensus sequence Tyr1-Ser2-Pro3-Thr4-Ser5-Pro6-Ser7 at the C-terminus (CTD) of its largest subunit (Rpb1). Dynamic phosphorylation patterns of serine residues in CTD during gene transcription coordinate the recruitment of factors to the elongating RNAPII and to the nascent transcript. Recent studies identified threonine 4 and tyrosine 1 as new CTD modifications and thereby expanded the "CTD code". In this review, we focus on CTD phosphorylation and its function in the RNAPII transcription cycle. We also discuss in detail the limitations of the phosphospecific CTD antibodies, which are used in all studies. This article is part of a Special Issue entitled: RNA Polymerase II Transcript Elongation.

Original languageEnglish
Pages (from-to)55-62
Number of pages8
JournalBiochimica et Biophysica Acta - Gene Regulatory Mechanisms
Volume1829
Issue number1
DOIs
StatePublished - Jan 2013
Externally publishedYes

Keywords

  • Carboxy-terminal domain
  • Phosphorylation
  • Posttranslational modification
  • RNA polymerase II
  • Transcription

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