The σ70 subunit of RNA polymerase is contacted by the λQ antiterminator during early elongation

Bryce Nickels, Christine W. Roberts, Haitao Sun, Jeffrey W. Roberts, Ann Hochschild

Research output: Contribution to journalArticle

46 Citations (Scopus)

Abstract

The Q protein of bacteriophage λ is a transcription antiterminator that modifies the elongation properties of E. coli RNA polymerase (RNAP). To do this, DNA-bound λQ must first engage a paused elongation complex. Here we show that this engagement of λQ with RNAP involves an interaction between λQ and σ70, demonstrating that σ70 can be a target of regulation during elongation. Furthermore, we provide evidence that this interaction between λQ and σ70 stabilizes a conformation of RNAP that requires the disengagement of a segment of σ70 from the core enzyme. Recent structure-based models posit that the transition from the initiation to the elongation phase of transcription involves the staged displacement of σ70 from the RNAP core. Our findings provide support for this proposal.

Original languageEnglish (US)
Pages (from-to)611-622
Number of pages12
JournalMolecular cell
Volume10
Issue number3
DOIs
StatePublished - Sep 1 2002
Externally publishedYes

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DNA-Directed RNA Polymerases
Bacteriophages
Escherichia coli
DNA
Enzymes
Proteins

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cell Biology

Cite this

Nickels, Bryce ; Roberts, Christine W. ; Sun, Haitao ; Roberts, Jeffrey W. ; Hochschild, Ann. / The σ70 subunit of RNA polymerase is contacted by the λQ antiterminator during early elongation. In: Molecular cell. 2002 ; Vol. 10, No. 3. pp. 611-622.
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The σ70 subunit of RNA polymerase is contacted by the λQ antiterminator during early elongation. / Nickels, Bryce; Roberts, Christine W.; Sun, Haitao; Roberts, Jeffrey W.; Hochschild, Ann.

In: Molecular cell, Vol. 10, No. 3, 01.09.2002, p. 611-622.

Research output: Contribution to journalArticle

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