Structure of the yeast RNA polymerase II holoenzyme: Mediator conformation and polymerase interaction

Joshua A. Davis, Yuichiro Takagi, Roger D. Kornberg, Francisco J. Asturias

Research output: Contribution to journalArticle

167 Scopus citations

Abstract

The holoenzyme formed by RNA polymerase II (RNAPII) and the Mediator complex is the target of transcriptional regulators in vivo. A three-dimensional structure of the yeast holoenzyme has been generated from electron microscopic images of single holoenzyme particles. Extensive changes in Mediator conformation required for interaction with RNAPII have been modeled by correlating the polymerase-bound and free Mediator structures. Determination of the precise orientation of the RNAPII in the holoenzyme indicates that Mediator contacts are centered on the RNAPII Rpb3/Rpb11 heterodimer, the eukaryotic homolog of the α2 homodimer involved in transcription regulation in prokaryotes. Implications for the possible mechanism of transcription regulation by Mediator are discussed.

Original languageEnglish (US)
Pages (from-to)409-415
Number of pages7
JournalMolecular Cell
Volume10
Issue number2
DOIs
StatePublished - Aug 2002
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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