Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2188450 | Journal of Molecular Biology | 2007 | 9 Pages |
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.
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Authors
Michaeleen Doucleff, Jeffrey G. Pelton, Peter S. Lee, B. Tracy Nixon, David E. Wemmer,