Structural Basis of DNA Recognition by the Alternative Sigma-factor, σ54

Michaeleen Doucleff, Jeffrey G. Pelton, Peter S. Lee, B. Tracy Nixon, David E. Wemmer

Research output: Contribution to journalArticlepeer-review

31 Scopus citations

Abstract

The σ subunit of bacterial RNA polymerase (RNAP) regulates gene expression by directing RNAP to specific promoters. Unlike σ70-type proteins, the alternative σ factor, σ54, requires interaction with an ATPase to open DNA. We present the solution structure of the C-terminal domain of σ54 bound to the -24 promoter element, in which the conserved RpoN box motif inserts into the major groove of the DNA. This structure elucidates the basis for sequence specific recognition of the -24 element, orients σ54 on the promoter, and suggests how the C-terminal domain of σ54 interacts with RNAP.

Original languageEnglish (US)
Pages (from-to)1070-1078
Number of pages9
JournalJournal of Molecular Biology
Volume369
Issue number4
DOIs
StatePublished - Jun 15 2007

All Science Journal Classification (ASJC) codes

  • Structural Biology
  • Molecular Biology

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