Analysis of heat and cold shock proteins in Listeria by two‐dimensional electrophoresis
- 1 January 1995
- journal article
- research article
- Published by Wiley in Electrophoresis
- Vol. 16 (1), 444-450
- https://doi.org/10.1002/elps.1150160172
Abstract
The proteins induced by heat and cold shock in Listeria monocytogenes (pathogenic for humans) and L. innocua (nonpathogenic) strains were analyzed by two-dimensional (2-D) electrophoresis with the help of a computerized 2-D gel analysis system. Heat (49°C) and cold (4°C) shock repressed roughly half the number of proteins synthesized at normal temperature (25°C) and decreased the level of numerous other proteins. Conversely, the synthesis of a great number of proteins was enhanced and novel proteins appeared upon temperature stress. There were more proteins induced in the L. monocytogenes strain than in the L. innocua strain. Each stress induced a set of specific proteins. There was overlap between these sets of proteins induced by heat and cold shock. Furthermore, a number of heat or cold shock proteins were found to be induced in both Listeria species and by both heat and cold shock in both species. The induction by heat shock was more intense than that by cold shock. The most strongly induced common stress protein of Listeria had a molecular mass of 17.6 kDa and an isoelectric point of 5.1.Keywords
This publication has 31 references indexed in Scilit:
- Differential heat-shock protein synthesis and response to stress in three avirulent and virulent listeria speciesResearch in Immunology, 1993
- Cloning, mapping and nucleotide sequencing of a gene encoding a universal stress protein in Eschericha coliMolecular Microbiology, 1992
- The effect of acid shock on the heat resistance of Listeria monocytogenesLetters in Applied Microbiology, 1992
- Molecular characterization of specific heat shock proteins inBacillus subtilisCurrent Microbiology, 1991
- Heat shock proteins and the immune responseImmunology Today, 1990
- Amino Acid Requirement of Six Strains of Listeria monocytogenesZentralblatt für Bakteriologie, 1989
- Abnormal Proteins Serve as Eukaryotic Stress Signals and Trigger the Activation of Heat Shock GenesScience, 1986
- Transient rates of synthesis of individual polypeptides in E. coli following temperature shiftsCell, 1978
- High resolution two-dimensional electrophoresis of basic as well as acidic proteinsCell, 1977
- Dependency on Medium and Temperature of Cell Size and Chemical Composition during Balanced Growth of Salmonella typhimuriumJournal of General Microbiology, 1958