Abstract
Examination of the binding of FeBABE-conjugated BvgA to the fha promoter of Bordetella pertussis has revealed that three dimers, formed by head-to-head association of monomers, bind one face of the DNA helix from the inverted-heptad primary binding site to the -35 region. The orientation of BvgA monomers within the dimers is the same as that recently demonstrated by X-ray crystallographic methods for a dimer of the C-terminal domain of NarL bound to DNA. Use of FeBABE conjugates of RNAP alpha subunit C-terminal domain showed that binding of this domain is linearly coincident with binding of the BvgA dimers, but to a different helical face. These results reveal a previously undescribed mode of interaction between RNAP alpha-CTD and a transcriptional activator.
MeSH terms
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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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Base Sequence
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Bordetella pertussis / genetics
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Bordetella pertussis / metabolism
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Cysteine / chemistry
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Cysteine / metabolism
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DNA / metabolism*
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DNA-Directed RNA Polymerases / chemistry
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DNA-Directed RNA Polymerases / genetics
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DNA-Directed RNA Polymerases / metabolism*
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Dimerization
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Models, Molecular
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Mutagenesis, Site-Directed
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Promoter Regions, Genetic*
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Protein Subunits / metabolism
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Transcription Factors / chemistry
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Transcription Factors / genetics
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Transcription Factors / metabolism*
Substances
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Bacterial Proteins
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BvgA protein, Bacteria
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Protein Subunits
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Transcription Factors
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DNA
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DNA-Directed RNA Polymerases
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RNA polymerase alpha subunit
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Cysteine