Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?

POTTER, Laura C.; MILLINGTON, Paul; GRIFFITHS, Lesley; THOMAS, Gavin H.; COLE, Jeffrey A.

doi:10.1042/bj3440077

Cited by 160Bacterial Genetics and BiotechnologyEscherichia coli research studiesWastewater Treatment and Nitrogen Removal

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Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?

POTTER, Laura C., MILLINGTON, Paul, GRIFFITHS, Lesley, THOMAS, Gavin H., COLE, Jeffrey A.·1999·Biochemical Journal

DOI 10.1042/bj3440077

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Abstract

The physiological role of the periplasmic nitrate reductase, Nap, one of the three nitrate reductases synthesized by Escherichia coli K-12, has been investigated. A series of double mutants that express only one nitrate reductase were grown anaerobically in batch cultures with glycerol as the non-fermentable carbon source and nitrate as the terminal electron acceptor. Only the strain expressing nitrate reductase A grew rapidly under these conditions. Introduction of a narL mutation severely decreased the growth rate of the nitrate reductase A strain, but enhanced the growth of the Nap+ strain. The ability to use nitrate as a terminal electron acceptor for anaerobic growth is therefore regulated primarily by the NarL protein at the level of transcription. Furthermore, the strain expressing nitrate reductase A had a substantial selective advantage in competition with the strain expressing only Nap during nitrate-sufficient continuous culture. However, the strain expressing Nap was preferentially selected during nitrate-limited continuous growth. The saturation constants for nitrate for the two strains (which numerically are equal to the nitrate concentrations at half of the maximum specific growth rate and therefore reflect the relative affinities for nitrate) were estimated using the integrated Monod equation to be 15 and 50 μM for Nap and nitrate reductase A respectively. This difference is sufficient to explain the selective advantage of the Nap+ strain during nitrate-limited growth. It is concluded that one physiological role of the periplasmic nitrate reductase of enteric bacteria is to enable bacteria to scavenge nitrate in nitrate-limited environments.

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nap is maximally expressed under low oxygen and low nitrate conditions, a difference suggested to possibly relate to a selective advantage over nar in the distal GI tract.
“it is notable that nap is maximally expressed under low oxygen and low nitrate conditions, a difference suggested to possibly relate to a selective advantage over nar in the distal GI tract[77,265].”
From Enterosalivary nitrate metabolism and the microbiome: Intersection of microbial metabolism, nitric oxide and diet in cardiac and pulmonary vascular health (2017) · cites this paper as [265]
NapB is an essential component of electron transport in organisms where it is present.
“This small c-type cytochrome is an essential component of electron transport in organisms where it is present.101,105”
From Nitrate and periplasmic nitrate reductases (2014) · cites this paper as [101]

Molecular cloning: A laboratory manual
Deininger, P. L. (1990) · Analytical Biochemistry · doi:10.1016/0003-2697(90)90595-z · Cited by 84,684
Construction and characterization of new cloning vehicles. II. A multipurpose cloning system.
Bolivar, F., Rodriguez, R. L., Greene, P. J., Betlach, M. C., Heyneker, H. L., Boyer, H. W., Crosa, J. H., & Falkow, S. (1977) · PubMed · Cited by 2,750
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Revsbech, N. P., & Sørensen, J. (1990) · Springer eBooks · doi:10.1007/978-1-4757-9969-9 · Cited by 256
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Authors: POTTER, L. C., MILLINGTON, P., GRIFFITHS, L., THOMAS, G. H., & COLE, J. A.
Affiliations: University of Birmingham (GB)
ORCID: THOMAS, Gavin H.
COLE, Jeffrey A.
Venue: Biochemical Journal
Publisher: Portland Press Ltd.
Published: 1999-11-08
Volume: 344
Issue: 1
Pages: 77-84
ISSN: 0264-6021 (ISSN-L)
1470-8728
DOI: 10.1042/bj3440077
OpenAlex: W7214186159
Cited by: 2
References: 4
Citations by year: 2021: 1 · 2016: 1
FWCI: 0.00
Type: journal article
Language: en
Open access: closed
Locations: Biochemical Journal (publishedVersion)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
Life Sciences › Immunology and Microbiology › Microbiology › Escherichia coli research studies
Physical Sciences › Environmental Science › Pollution › Wastewater Treatment and Nitrogen Removal
Keywords: Escherichia coli, periplasmic nitrate reductase, NAP, NarL, competitive growth, anaerobic growth, transcriptional regulation, glycerol carbon source

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Competition between Escherichia coli strains expressing either a periplasmic or a membrane-bound nitrate reductase: does Nap confer a selective advantage during nitrate-limited growth?

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