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• W1994565715 endingPage "3568" @default.
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• W1994565715 abstract "Transcription initiation by bacterial σ(54)-polymerase requires the action of a transcriptional activator protein. Activators bind sequence-specifically upstream of the transcription initiation site via a DNA-binding domain (DBD). The structurally characterized DBDs from activators all belong to the Fis (factor for inversion stimulation) family of helix-turn-helix DNA-binding proteins. We report here structures of the free and DNA-bound forms of the DBD of NtrC4 (4DBD) from Aquifex aeolicus, a member of the NtrC family of σ(54) activators. Two NtrC4-binding sites were identified upstream (-145 and -85bp) from the start of the lpxC gene, which is responsible for the first committed step in lipid A biosynthesis. This is the first experimental evidence for σ(54) regulation in lpxC expression. 4DBD was crystallized both without DNA and in complex with the -145-binding site. The structures, together with biochemical data, indicate that NtrC4 binds to DNA in a manner that is similar to that of its close homolog, Fis. The greater sequence specificity for the binding of 4DBD relative to Fis seems to arise from a larger number of base-specific contacts contributing to affinity than for Fis." @default.
• W1994565715 created "2016-06-24" @default.
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• W1994565715 date "2014-10-01" @default.
• W1994565715 modified "2023-10-10" @default.
• W1994565715 title "DNA Recognition by a σ54 Transcriptional Activator from Aquifex aeolicus" @default.
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• W1994565715 doi "https://doi.org/10.1016/j.jmb.2014.08.009" @default.
• W1994565715 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4188747" @default.
• W1994565715 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/25158097" @default.
• W1994565715 hasPublicationYear "2014" @default.
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