Protein synthesis patterns in Acinetobacter calcoaceticus induced by phenol and catechol show specificities of responses to chemostress.
The proteins induced in Acinetobacter calcoaceticus by the potentially toxic growth substrates phenol and catechol were analyzed by 2D-electrophoresis of cell extracts and compared with those induced by heat shock and oxidative stress. Although both aromatic compounds are quite similar, the only difference being that catechol has an additional hydroxyl group, the responses obtained differed considerably. Phenol has greater lipophilicity and mainly induced heat shock proteins, whereas catechol, which causes the production of reactive oxygen species, predominantly induced oxidative stress proteins. Furthermore, some special proteins were induced by phenol or catechol, which might be useful as biomarkers for chemostress, and could be involved in the catalytic degradation of potentially toxic compounds.
Benndorf
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Umweltforschungszentrum Leipzig-Halle GmbH, Sektion Umweltmikrobiologie, Permoserstr. 15, 04318, Leipzig, Germany.
Loffhagen
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N
Babel
W
W
D016954:Acinetobacter calcoaceticus / Q000187:drug effects* / Q000254:growth & development / Q000378:metabolism; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000187:drug effects; D002374:Catalase / Q000378:metabolism; D002396:Catechols / Q000494:pharmacology*; D002470:Cell Survival / Q000187:drug effects; D015180:Electrophoresis, Gel, Two-Dimensional; D006358:Hot Temperature; D006861:Hydrogen Peroxide / Q000494:pharmacology; D010636:Phenols / Q000494:pharmacology*
D001426:Bacterial Proteins; D002396:Catechols; D010636:Phenols; D006861:Hydrogen Peroxide; D002374:Catalase; C034221:catechol