Structures of RNA Polymerase Closed and Intermediate Complexes Reveal Mechanisms of DNA Opening and Transcription Initiation

Robert Glyde, Fuzhou Ye, Vidya Chandran Darbari, Nan Zhang, Martin Buck, Xiaodong Zhang

Research output: Contribution to journalArticle

20 Scopus citations

Abstract

Gene transcription is carried out by RNA polymerases (RNAPs). For transcription to occur, the closed promoter complex (RPc), where DNA is double stranded, must isomerize into an open promoter complex (RPo), where the DNA is melted out into a transcription bubble and the single-stranded template DNA is delivered to the RNAP active site. Using a bacterial RNAP containing the alternative σ54 factor and cryoelectron microscopy, we determined structures of RPc and the activator-bound intermediate complex en route to RPo at 3.8 and 5.8 Å. Our structures show how RNAP-σ54 interacts with promoter DNA to initiate the DNA distortions required for transcription bubble formation, and how the activator interacts with RPc, leading to significant conformational changes in RNAP and σ54 that promote RPo formation. We propose that DNA melting is an active process initiated in RPc and that the RNAP conformations of intermediates are significantly different from that of RPc and RPo.

Original languageEnglish (US)
Pages (from-to)106-116.e4
JournalMolecular Cell
Volume67
Issue number1
DOIs
StatePublished - Jul 6 2017

Keywords

  • AAA protein
  • DNA distortion
  • DNA opening
  • RNA polymerase
  • sigma factor
  • sigma54
  • transcription bubble
  • transcription closed complex
  • transcription initiation
  • transcription intermediate complex

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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