Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2,5, and 7

Minkyu Kim, Hyunsuk Suh, Eun Jung Cho, Stephen Buratowski

Research output: Contribution to journalArticlepeer-review

109 Scopus citations

Abstract

The C-terminal domain (CTD) of Rpb1, the largest subunit of RNA polymerase II, acts as a binding platform for various mRNA processing and histone-modifying enzymes that act cotranscriptionally. These factors are targeted to specific phosphorylation states of the CTD that predominate at different stages of transcription. Within the repeating sequence YSPTSPS, serines 2 and 5 are major phosphorylation sites, but serine 7 phosphorylation was recently discovered in mammalian cells. Here we show that CTD serine 7 is also phosphorylated in yeast and that Ser-7(P) chromatin immunoprecipitation patterns resemble those of Ser-5(P). The basal factor TFIIH can phosphorylate Ser-7 in vitro and is necessary for Ser-7(P) in vivo. Interestingly, deletion of the CTD Ser-5(P) phosphatase Rtr1 leads to an increase in Ser-5(P) but not Ser-7(P).

Original languageEnglish (US)
Pages (from-to)26421-26426
Number of pages6
JournalJournal of Biological Chemistry
Volume284
Issue number39
DOIs
StatePublished - Sep 25 2009
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Phosphorylation of the yeast Rpb1 C-terminal domain at serines 2,5, and 7'. Together they form a unique fingerprint.

Cite this