Structural basis of DNA recognition by the alternative sigma-factor, sigma54 |
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Authors: | Doucleff Michaeleen Pelton Jeffrey G Lee Peter S Nixon B Tracy Wemmer David E |
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Institution: | Physical Biosciences Division, Lawrence Berkeley National Laboratory and the Department of Chemistry, University of California, Berkeley, CA 94720, USA. |
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Abstract: | The sigma subunit of bacterial RNA polymerase (RNAP) regulates gene expression by directing RNAP to specific promoters. Unlike sigma(70)-type proteins, the alternative sigma factor, sigma(54), requires interaction with an ATPase to open DNA. We present the solution structure of the C-terminal domain of sigma(54) 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 sigma(54) on the promoter, and suggests how the C-terminal domain of sigma(54) interacts with RNAP. |
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Keywords: | HTH helix-turn-helix r m s d root-mean-square deviation RNAP RNA polymermase s d standard deviation wHTH winged-helix-turn-helix NOESY nuclear Overhauser enhancement spectroscopy TOCSY total correlated spectroscopy |
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