Transcriptomics

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The PAS domain of the Polarly-Localized Histidine Kinase FlrB in Vibrio cholerae Controls Class III Flagellar Transcription and Contributes to Intestinal Colonization


ABSTRACT: FlrB is a histidine kinase and along with FlrC it represents the two-component system that regulates flagellar transcription within Vibrio cholerae. FlrB autophosphorylates the conserved histidine at amino acid position 135, then transfers the phosphate to the conserved aspartate residue at position 54 in FlrC. FlrC-P binds promoter regions and activates sigma54-dependent transcription of class III flagellar genes. By mutating the histidine at position 135 to an asparagine (H135N), FlrB is unable to undergo autophosphorylation, prohibiting phosphorylation of FlrC and transcription of FlrC-dependent genes. Mutating the leucine residue at position 36 in the PAS domain of FlrB to a phenylalanine (L36F) results in increased FlrC-dependent transcription. We hypothesize that V. cholerae with the FlrB L36F mutant form produces significantly higher amounts of FlrC-dependent transcripts. Conversely, FlrB H135N mutants will be significantly downregulated for the same genes.

ORGANISM(S): Vibrio cholerae O395

PROVIDER: GSE302736 | GEO | 2025/08/07

REPOSITORIES: GEO

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