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Volume 148, Issue 9

Assimilatory detoxification of herbicides by MC1: induction of two chlorocatechol 1,2-dioxygenases as a response to chemostress

The SWISS-PROT accession numbers for the sequences reported in this paper are P83115, P83116 and P83117.

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Abstract

Proteome analysis of bacteria that can detoxify harmful organic compounds enables the discovery of enzymes involved in the biodegradation of these substances and proteins that protect the cell against poisoning. Exposure of MC1 to 2,4-dichlorophenoxypropionic acid and its metabolites 2,4-dichlorophenol and 3,5-dichlorocatechol during growth on pyruvate as a source of carbon and energy induced several proteins. Contrary to the general hypothesis that lipophilic or reactive compounds induce heat shock or oxidative stress proteins, no induction of the GroEL, DnaK and AhpC proteins that were used as markers for the induction of heat shock and oxidative stress responses was observed. However, two chlorocatechol1,2-dioxygenases, identified by amino terminal sequence analysis, were induced. Both enzymes catalyse the conversion of 3,5-dichlorocatechol to 2,4-dichloro-,-muconate indicating that biodegradation is a major mechanism of resistance in the detoxifying bacterium MC1.

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Keyword(s): 2,4-DCP, 2,4-dichlorophenol , 2,4-DCPP, 2,4-dichlorophenoxypropionic acid , 2D-PAGE , 3,5-DCC, 3,5-dichlorocatechol , chlorophenoxy herbicides , degradation , IPG, immobilized pH gradient and resistance mechanism
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2002-09-01
2024-04-23
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Assimilatory detoxification of herbicides by Delftia acidovorans MC1: induction of two chlorocatechol 1,2-dioxygenases as a response to chemostressThe SWISS-PROT accession numbers for the sequences reported in this paper are P83115, P83116 and P83117.
Microbiology 148, 2883 (2002); https://doi.org/10.1099/00221287-148-9-2883
/content/journal/micro/10.1099/00221287-148-9-2883
/content/journal/micro/10.1099/00221287-148-9-2883
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