Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity

Bell, L. C., Page, M. D., Berks, B. C., Richardson, D. J. ORCID: https://orcid.org/0000-0002-6847-1832 and Ferguson, S. J. (1993) Insertion of transposon Tn5 into a structural gene of the membrane-bound nitrate reductase of Thiosphaera pantotropha results in anaerobic overexpression of periplasmic nitrate reductase activity. Journal of General Microbiology, 139 (12). pp. 3205-3214. ISSN 0022-1287

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Abstract

Chlorate-resistant mutants of the denitrifying bacterium Thiosphaera pantotropha were generated by transposon Tn5 mutagenesis. One class was deficient in membrane-bound nitrate reductase activity but retained a periplasmic nitrate reductase activity. Using transposon marker rescue it was shown that in one such mutant, M-6, the transposon was inserted in the membrane-bound nitrate reductase β subunit structural gene (termed narH in order to be consistent with the nomenclature of the Escherichia coli major nitrate reductase operon). The translated sequence (total of 106 amino acids) from around the point of transposon insertion showed approximately 90% amino acid identity with the β subunits of the E. coli nitrate reductases. Under anaerobic growth conditions M-6 overproduced the periplasmic nitrate reductase activity allowing anaerobic growth with nitrate as electron acceptor. A regulatory link was inferred between the presence of the membrane-bound nitrate reductase and expression of the periplasmic nitrate reductase. This is the first demonstration of full denitrification in an organism possessing only a periplasmic nitrate reductase.

Item Type: Article
Uncontrolled Keywords: microbiology ,/dk/atira/pure/subjectarea/asjc/2400/2404
Faculty \ School:
Faculty of Science > School of Biological Sciences
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Depositing User: LivePure Connector
Date Deposited: 15 Jul 2022 12:31
Last Modified: 13 Aug 2022 02:20
URI: https://ueaeprints.uea.ac.uk/id/eprint/86207
DOI: 10.1099/00221287-139-12-3205

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