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Titre :
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Cold shock and cold acclimation proteins in the psychrotrophic bacterium Arthrobacter globiformis SI 55
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Auteurs :
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F. Berger ;
N. Morellet ;
CEMAGREF NOGENT SUR VERNISSON ENNO ;
F. Menu ;
P. Potier
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Type de document :
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article/chapitre/communication
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Année de publication :
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1996
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Format :
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p. 2999-3007
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Note générale :
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Sigle : CEMAGREF
Sigle : ENNO
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Langues:
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= Anglais
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Catégories :
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Divers
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Mots-clés:
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BACTERIE
;
PROTEINE
;
RESISTANCE A LA TEMPERATURE
;
ANALYSE PHYSICOCHIMIQUE
;
ANALYSE BIOCHIMIQUE
;
ELECTROPHORESE
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Résumé :
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The psychrotrophic bacterium Arthrobacter globiformis SI55 was grown at 4 ant 25°C, and the cell protein contents were analyzed by two-dimensional electrophoresis. Cells subjected to cold shocks of increasing magnitude were also analyzed. Correspondence analysis of protein appearance distinguished four groups of physiological significance. Group I contained cold shock proteins (Csps) overexpressed only after a large temperature downshift. Group II contained Csps with optimal expression after mild shocks. Group III contained proteins overexpressed after all cold shocks. These last proteins were also overexpressed in cells growing at 4° C and were considered to be early cold acclimation proteins (Caps). Group IV contained proteins which were present at high concentrations only in 4°C steady-state cells and appeared to be late Caps. A portion of a gene very similar to the Escherichia coli cspA gene (encoding protein CS7.4) was identified. A synthetic peptide was used to produce an antibody which detected a CS7.4-like protein (A9) by immunoblotting two-dimensional electrophoresis gels of A. globiformis SI55 total proteins. Unlike mesophilic microoganisms, this CS7.4-like protein was still produced during prolonged growth at low temperature, and it might have a particular adaptive function needed for balanced growth under harsh conditions. However, A9 was induced at high temperature by chloramphenicol, suggesting that CS7.4-like proteins have a more general role than their sole implication in cold acclimation processes.
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Source :
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Journal of bacteriology, vol. 178, n°11
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