Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.
Hsp31, the product of the sigmaS - and sigmaD -dependent hchA gene, is a heat-inducible chaperone implicated in the management of protein misfolding at high temperatures. We show here that Hsp31 plays an important role in the acid resistance of starved Escherichia coli but that it has little influence on oxidative-stress survival.
Mujacic
Mirna
M
Department of Bioengineering, University of Washington, Box 351750, Seattle, WA 98195-1750, USA.
Baneyx
François
F
D024881:Drug Resistance, Bacterial; D004926:Escherichia coli / Q000187:drug effects / Q000254:growth & development* / Q000502:physiology*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D018869:Heat-Shock Response; D006851:Hydrochloric Acid / Q000494:pharmacology*; D006863:Hydrogen-Ion Concentration; D018832:Molecular Chaperones / Q000235:genetics / Q000378:metabolism*; D018384:Oxidative Stress
D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C469996:hchA protein, E coli; D006851:Hydrochloric Acid