title: Chaperone Hsp31 contributes to acid resistance in stationary-phase Escherichia coli.
abstract: 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.
authors.affiliation: Department of Bioengineering, University of Washington, Box 351750, Seattle, WA 98195-1750, USA.
authors.forename: Mirna
authors.initials: M
authors.lastname: Mujacic
authors.forename: François
authors.initials: F
authors.lastname: Baneyx
mesh_terms: 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
chemical_list: D029968:Escherichia coli Proteins; D018832:Molecular Chaperones; C469996:hchA protein, E coli; D006851:Hydrochloric Acid