Cooperative interaction of transcription termination factors with the RNA polymerase II C-terminal domain

Bradley M. Lunde, Steve L. Reichow, Minkyu Kim, Hyunsuk Suh, Thomas C. Leeper, Fan Yang, Hannes Mutschler, Stephen Buratowski, Anton Meinhart, Gabriele Varani

Research output: Contribution to journalArticlepeer-review

113 Scopus citations

Abstract

Phosphorylation of the C-terminal domain (CTD) of RNA polymerase II controls the co-transcriptional assembly of RNA processing and transcription factors. Recruitment relies on conserved CTD-interacting domains (CIDs) that recognize different CTD phosphoisoforms during the transcription cycle, but the molecular basis for their specificity remains unclear. We show that the CIDs of two transcription termination factors, Rtt103 and Pcf11, achieve high affinity and specificity both by specifically recognizing the phosphorylated CTD and by cooperatively binding to neighboring CTD repeats. Single-residue mutations at the protein-protein interface abolish cooperativity and affect recruitment at the 3′ end processing site in vivo. We suggest that this cooperativity provides a signal-response mechanism to ensure that its action is confined only to proper polyadenylation sites where Ser2 phosphorylation density is highest.

Original languageEnglish (US)
Pages (from-to)1195-1201
Number of pages7
JournalNature Structural and Molecular Biology
Volume17
Issue number10
DOIs
StatePublished - Oct 2010
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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