title: A grpE mutant of Escherichia coli is more resistant to heat than the wild-type.
abstract: The grpE gene of Escherichia coli is essential for bacteriophage lambda DNA replication and is also necessary for host RNA and DNA synthesis at high temperature. A grpE mutant of E. coli was found to be substantially more resistant to 50 degrees C heat treatment than the wild-type. Upon receiving a 42 degrees C heat shock for 15 min, both the wild-type and the grpE mutant became more resistant to heat (i.e. they became thermotolerant). A grpE+ revertant behaved similarly to the wild-type in that it was more sensitive to heat than grpE cells. In addition, grpE cells had the same H2O2 and UV sensitivity as the wild-type. This implies that the conditions for which a grpE mutation is beneficial are unique to heat exposure and are not caused by H2O2 or UV exposure. Furthermore, synthesis of heat-shock proteins occurred sooner in the grpE mutant than in the wild-type, indicating that the grpE gene of E. coli may influence the regulation of the heat-shock response.
authors.affiliation: Department of Microbiology and Immunology, College of Medicine, University of Arizona, Tucson 85724.
authors.forename: J M
authors.initials: JM
authors.lastname: Delaney
mesh_terms: D001426:Bacterial Proteins / Q000096:biosynthesis / Q000235:genetics; D010582:Bacteriophage lambda / Q000235:genetics; D004261:DNA Replication / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics* / Q000378:metabolism; D005798:Genes, Bacterial; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000235:genetics; D006358:Hot Temperature; D009154:Mutation
chemical_list: D001426:Bacterial Proteins; D006360:Heat-Shock Proteins