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• W1570731023 abstract "H-NS is an abundant bacterial protein involved in transcriptional silencing of a variety of environmentally responsive genes during growth under non-permissive conditions. We have previously demonstrated a direct role for H-NS in the negative modulation of expression of several genes within the ToxR virulence regulon of Vibrio cholerae. Here we have undertaken extensive mutagenesis of the structural and functional domains of the H-NS protein to determine the contribution of each to the regulation of gene expression. Insertions within, or truncations of, the C-terminal conserved DNA-binding domain prevent repression of toxT and ctx, as expected. Dominant negative experiments demonstrate that V. cholerae H-NS represses gene expression as an oligomeric protein. Hydrophobic coiledcoil interactions have been shown to provide oligomerization capability in other H-NS orthologues. We used site-directed mutagenesis to construct altered V. cholerae H-NS proteins, including an extensive internal deletion within the predicted coiledcoil domain. Remarkably, these proteins were competent to repress gene expression and to form oligomers. Chimeric H-NS proteins, using sequences from both Escherichia coli and V. cholerae H-NS orthologues, revealed that V. cholerae H-NS possesses a second oligomerization domain in the N-terminal 24 amino acids of the protein. Overall, our results suggest DNA binding and protein oligomerization, provided by either the central coiledcoil or N-terminal domain, are required for repression of promoters responsive to H-NS within the ToxR regulon." @default.
• W1570731023 created "2016-06-24" @default.
• W1570731023 creator A5028919850 @default.
• W1570731023 creator A5033034795 @default.
• W1570731023 date "2003-08-27" @default.
• W1570731023 modified "2023-09-29" @default.
• W1570731023 title "Vibrio cholerae H-NS domain structure and function with respect to transcriptional repression of ToxR regulon genes reveals differences among H-NS family members" @default.
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• W1570731023 doi "https://doi.org/10.1046/j.1365-2958.2003.03701.x" @default.
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