Acid shock proteins of Escherichia coli.
Synthesis of total cellular proteins of Escherichia coli was studied after transfer of cultures from pH 6.9 to pH 4.3. Proteins induced by such an external pH shift down were identified by mono- and bi-dimensional electrophoresis. 30 to 45 min after an acid shift, a group of at least sixteen polypeptides was markedly induced. Four of these polypeptides corresponded to the well known heat shock proteins GroEL, DnaK, HtpG and HtpM. Their pH induction was RpoH-dependent. Three other pH-induced proteins were previously identified as stress proteins induced either by osmolarity or aerobiosis or low temperature (proteins 32 (defined in this paper), C70.0 and C62.7). Seven other proteins were specifically induced after an acid shift and were called acid shock proteins (ASP). The induction of one of these proteins was RpoH-dependent, whereas that of others was RpoH-independent.
Laboratoire de Microbiologie et Génétique Moléculaire, Université Claude Bernard Lyon I, Villeurbanne, France.
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Heyde
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Portalier
D001426:Bacterial Proteins / Q000096:biosynthesis / Q000378:metabolism*; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004591:Electrophoresis, Polyacrylamide Gel; D004926:Escherichia coli / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000096:biosynthesis / Q000378:metabolism*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D013696:Temperature
D001426:Bacterial Proteins; D006360:Heat-Shock Proteins; D012321:DNA-Directed RNA Polymerases