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.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Bacterial Proteins / chemistry*
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Bacterial Proteins / genetics
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Bacterial Proteins / metabolism*
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DNA* / chemistry
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DNA* / metabolism
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DNA-Directed RNA Polymerases / genetics
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DNA-Directed RNA Polymerases / metabolism
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Gene Expression Regulation, Bacterial
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Macromolecular Substances
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Models, Molecular
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Molecular Sequence Data
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Nuclear Magnetic Resonance, Biomolecular
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Nucleic Acid Conformation
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Promoter Regions, Genetic
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Protein Binding
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Protein Conformation
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RNA Polymerase Sigma 54 / chemistry*
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RNA Polymerase Sigma 54 / genetics
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RNA Polymerase Sigma 54 / metabolism*
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Sequence Alignment
Substances
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Bacterial Proteins
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Macromolecular Substances
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DNA
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DNA-Directed RNA Polymerases
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RNA Polymerase Sigma 54
Associated data
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GENBANK/AAC06814
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PDB/2O8K
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PDB/2O9L