1. Heat Shock Protein-Mediated Resistance to High Hydrostatic Pressure in Escherichia coli
- Author
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Anne Farewell, Philipp De Spiegeleer, Abram Aertsen, Kristel J. A. Hauben, Thomas Nyström, Chris W. Michiels, Kristof Vanoirbeek, and Jan Sermon
- Subjects
Green Fluorescent Proteins ,Hydrostatic pressure ,Biology ,medicine.disease_cause ,Applied Microbiology and Biotechnology ,Microbiology ,barotolerance ,yeast saccharomyces-cerevisiae ,Sigma factor ,Heat shock protein ,Escherichia coli ,Hydrostatic Pressure ,stress-proteins ,medicine ,salmonella-typhimurium ,Heat shock ,Promoter Regions, Genetic ,Heat-Shock Proteins ,deep-sea ,HSPA14 ,Ecology ,Escherichia coli Proteins ,induced cross protection ,Gene Expression Regulation, Bacterial ,Physiology and Biotechnology ,gene-expression ,Molecular biology ,Culture Media ,Luminescent Proteins ,Regulon ,membrane damage ,Shock (circulatory) ,bacteria ,swiss-2dpage database update ,medicine.symptom ,listeria-monocytogenes ,Heat-Shock Response ,Food Science ,Biotechnology - Abstract
A random library of Escherichia coli MG1655 genomic fragments fused to a promoterless green fluorescent protein (GFP) gene was constructed and screened by differential fluorescence induction for promoters that are induced after exposure to a sublethal high hydrostatic pressure stress. This screening yielded three promoters of genes belonging to the heat shock regulon ( dnaK , lon , clpPX ), suggesting a role for heat shock proteins in protection against, and/or repair of, damage caused by high pressure. Several further observations provide additional support for this hypothesis: (i) the expression of rpoH , encoding the heat shock-specific sigma factor σ 32 , was also induced by high pressure; (ii) heat shock rendered E. coli significantly more resistant to subsequent high-pressure inactivation, and this heat shock-induced pressure resistance followed the same time course as the induction of heat shock genes; (iii) basal expression levels of GFP from heat shock promoters, and expression of several heat shock proteins as determined by two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins extracted from pulse-labeled cells, was increased in three previously isolated pressure-resistant mutants of E. coli compared to wild-type levels.
- Published
- 2004