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The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases

Marco Fischer, Jesse Alderson, Geertje Van Keulen, Janet White, R. Gary Sawers, Geertje Van Keulen Orcid Logo

Microbiology, Volume: 156, Issue: 10, Pages: 3166 - 3179

Swansea University Author: Geertje Van Keulen Orcid Logo

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DOI (Published version): 10.1099/mic.0.042572-0

Abstract

Streptomyces coelicolor A3(2) synthesizes three membrane-associated respiratory nitrate reductases (Nars). During aerobic growth in liquid medium the bacterium was able to reduce 50 mM nitrate stoichiometrically to nitrite. Construction and analysis of a mutant in which all three narGHJI operons wer...

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Published in: Microbiology
ISSN: 1350-0872 1465-2080
Published: Microbiology 2010
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URI: https://cronfa.swan.ac.uk/Record/cronfa9995
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spelling 2013-09-23T11:01:05.3096109 v2 9995 2012-03-21 The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases 6b2c798924ac19de63e2168d50b99425 0000-0002-6044-1575 Geertje Van Keulen Geertje Van Keulen true false 2012-03-21 BMS Streptomyces coelicolor A3(2) synthesizes three membrane-associated respiratory nitrate reductases (Nars). During aerobic growth in liquid medium the bacterium was able to reduce 50 mM nitrate stoichiometrically to nitrite. Construction and analysis of a mutant in which all three narGHJI operons were deleted showed that it failed to reduce nitrate. Deletion of the gene encoding MoaA, which catalyses the first step in molybdenum cofactor biosynthesis, also prevented nitrate reduction, consistent with the Nars being molybdoenzymes. In contrast to the triple narGHJI mutant, the moaA mutant was also unable to use nitrate as sole nitrogen source, which indicates that the assimilatory nitrate reductases in S. coelicolor are also molybdenum-dependent. Analysis of S. coelicolor growth on solid medium demonstrated that Nar activity is present in both spores and mycelium (hypha). Development of a survival assay with the nitrate analogue chlorate revealed that wild-type S. coelicolor spores and mycelium were sensitive to chlorate after anaerobic incubation, independent of the presence of nitrate, while both the moaA and triple nar mutants were chlorate-resistant. Complementation of the triple nar mutant with the individual narGHJI operons delivered on cosmids revealed that each operon encoded an enzyme that was synthesized and active in nitrate or chlorate reduction. The data obtained from these studies allow a tentative assignment of Nar1 activity to spores, Nar2 to spores and mycelium, and Nar3 exclusively to mycelium. Journal Article Microbiology 156 10 3166 3179 Microbiology 1350-0872 1465-2080 1 7 2010 2010-07-01 10.1099/mic.0.042572-0 http://mic.sgmjournals.org/content/156/10/3166.long COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2013-09-23T11:01:05.3096109 2012-03-21T16:17:13.0000000 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Marco Fischer 1 Jesse Alderson 2 Geertje Van Keulen 3 Janet White 4 R. Gary Sawers 5 Geertje Van Keulen 0000-0002-6044-1575 6
title The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
spellingShingle The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
Geertje Van Keulen
title_short The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
title_full The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
title_fullStr The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
title_full_unstemmed The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
title_sort The obligate aerobe Streptomyces coelicolor A3(2) synthesizes three active respiratory nitrate reductases
author_id_str_mv 6b2c798924ac19de63e2168d50b99425
author_id_fullname_str_mv 6b2c798924ac19de63e2168d50b99425_***_Geertje Van Keulen
author Geertje Van Keulen
author2 Marco Fischer
Jesse Alderson
Geertje Van Keulen
Janet White
R. Gary Sawers
Geertje Van Keulen
format Journal article
container_title Microbiology
container_volume 156
container_issue 10
container_start_page 3166
publishDate 2010
institution Swansea University
issn 1350-0872
1465-2080
doi_str_mv 10.1099/mic.0.042572-0
publisher Microbiology
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
url http://mic.sgmjournals.org/content/156/10/3166.long
document_store_str 0
active_str 0
description Streptomyces coelicolor A3(2) synthesizes three membrane-associated respiratory nitrate reductases (Nars). During aerobic growth in liquid medium the bacterium was able to reduce 50 mM nitrate stoichiometrically to nitrite. Construction and analysis of a mutant in which all three narGHJI operons were deleted showed that it failed to reduce nitrate. Deletion of the gene encoding MoaA, which catalyses the first step in molybdenum cofactor biosynthesis, also prevented nitrate reduction, consistent with the Nars being molybdoenzymes. In contrast to the triple narGHJI mutant, the moaA mutant was also unable to use nitrate as sole nitrogen source, which indicates that the assimilatory nitrate reductases in S. coelicolor are also molybdenum-dependent. Analysis of S. coelicolor growth on solid medium demonstrated that Nar activity is present in both spores and mycelium (hypha). Development of a survival assay with the nitrate analogue chlorate revealed that wild-type S. coelicolor spores and mycelium were sensitive to chlorate after anaerobic incubation, independent of the presence of nitrate, while both the moaA and triple nar mutants were chlorate-resistant. Complementation of the triple nar mutant with the individual narGHJI operons delivered on cosmids revealed that each operon encoded an enzyme that was synthesized and active in nitrate or chlorate reduction. The data obtained from these studies allow a tentative assignment of Nar1 activity to spores, Nar2 to spores and mycelium, and Nar3 exclusively to mycelium.
published_date 2010-07-01T03:11:29Z
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score 10.998116

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