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Analysis of heat and cold shock proteins in Listeria by two‐dimensional electrophoresis
Author(s) -
PhanThanh Luu,
Gormon Thierry
Publication year - 1995
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.1150160172
Subject(s) - isoelectric point , heat shock protein , gel electrophoresis , listeria monocytogenes , cold shock domain , molecular mass , isoelectric focusing , shock (circulatory) , heat shock , electrophoresis , listeria , strain (injury) , hspa14 , chemistry , biochemistry , polyacrylamide gel electrophoresis , biology , hsp70 , bacteria , genetics , rna , gene , enzyme , medicine , anatomy
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.