Escherichia coli mutants with altered control of alcohol dehydrogenase and nitrate reductase.

Journal of Bacteriology
D P Clark, J E Cronan

Abstract

Mutants of Escherichia coli which overproduce alcohol dehydrogenase were obtained by selection for the ability to use ethanol as an acetate source in a strain auxotrophic for acetate. A mutant having a 20-fold overproduction of alcohol dehydrogenase was able to use ethanol only to fulfill its acetate requirement, whereas two mutants with a 60-fold overproduction were able to use ethanol as a sole carbon source. The latter two mutants produced only 25% of the wild-type level of nitrate reductase, when grown under anaerobic conditions. Alcohol dehydrogenase production was largely unaffected by catabolite repression but was repressed by nitrate under both aerobic and anaerobic conditions. The genetic locus responsible for alcohol dehydrogenase overproduction was located at min 27 on the E. coli genetic map; the gene order, as determined by transduction, was trp tonB adh chlC hemA. The possible relationship of alcohol dehydrogenase to anaerobic redox systems such as formate-nitrate reductase is discussed.

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Citations

Jan 1, 1994·Critical Reviews in Microbiology·M F Reid, C A Fewson
Feb 1, 1997·FEMS Microbiology Letters·G VézinaM Boissinot
Oct 11, 2002·Proceedings of the National Academy of Sciences of the United States of America·Travis H TaniRowena G Matthews
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May 23, 2014·Molecular Microbiology·Katherine S H BeckhamAndrew J Roe
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Feb 26, 2015·PloS One·Todd T EckdahlE Tucker Whitesides
Nov 26, 1999·Journal of Bacteriology·J Membrillo-HernándezE C Lin
May 1, 2018·Applied Microbiology and Biotechnology·Jayashree Chakravarty, Christopher J Brigham
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Sep 1, 1984·Microbiological Reviews·W J Ingledew, R K Poole
Nov 1, 1982·Journal of Bacteriology·W Lorowitz, D Clark

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