The HOCl-specific transcription factor HypT mediates HOCl resistance in
E. coli. The reduced, inactive HypT forms an unusual dodecamer while the tetramer binds to target DNA. HypT is reversibly activated by HOCl by oxidation of three distinctive methionine residues to methionine sulfoxide. Cysteines are not involved in the regulation of HypT activity in vivo. Thus, HypT is a novel redox-regulated protein. Further, HOCl stress causes significant changes to the metabolism of
E. coli. such as alteration of the levels of the metabolites alanine, methionine, glucose, and formate.
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The HOCl-specific transcription factor HypT mediates HOCl resistance in
E. coli. The reduced, inactive HypT forms an unusual dodecamer while the tetramer binds to target DNA. HypT is reversibly activated by HOCl by oxidation of three distinctive methionine residues to methionine sulfoxide. Cysteines are not involved in the regulation of HypT activity in vivo. Thus, HypT is a novel redox-regulated protein. Further, HOCl stress causes significant changes to the metabolism of
E. coli. such as alter...
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