Regulation of denitrification genes in Neisseria meningitidis by nitric oxide and the repressor NsrR
Regulation of denitrification genes in Neisseria meningitidis by nitric oxide and the repressor NsrR
The human pathogen Neisseria meningitidis is capable of growth using the denitrification of nitrite to nitrous oxide under microaerobic conditions. This process is catalyzed by two reductases: nitrite reductase (encoded by aniA) and nitric oxide (NO) reductase (encoded by norB). Here, we show that in N. meningitidis MC58 norB is regulated by nitric oxide via the product of gene NMB0437 which encodes NsrR. NsrR is a repressor in the absence of NO, but norB expression is derepressed by NO in an NsrR-dependent manner. nsrR-deficient mutants grow by denitrification more rapidly than wild-type N. meningitidis, and this is coincident with the upregulation of both NO reductase and nitrite reductase even under aerobic conditions in the absence of nitrite or NO. The NsrR-dependent repression of aniA (unlike that of norB) is not lifted in the presence of NO. The role of NsrR in the control of expression of aniA is linked to the function of the anaerobic activator protein FNR: analysis of nsrR and fnr single and nsrR fnr double mutants carrying an aniA promoter lacZ fusion indicates that the role of NsrR is to prevent FNR-dependent aniA expression under aerobic conditions, indicating that FNR in N. meningitidis retains considerable activity aerobically.
Aerobiosis, Anaerobiosis, Bacterial Outer Membrane Proteins, Bacterial Proteins, Blotting, Western, Gene Expression Regulation, Bacterial, Genes, Bacterial, Mutation, Neisseria meningitidis, Nitric Oxide, Nitric Oxide Donors, Nitrite Reductases, Nitrites, Nitrous Oxide, Oxidoreductases, Recombinant Fusion Proteins, Repressor Proteins, Journal Article, Research Support, Non-U.S. Gov't
1138-1144
Rock, Jonathan D.
8e8fc55a-ebd8-4fcf-93e7-99b2909d34f0
Thomson, Melanie J.
a18b3a0f-1ec2-4928-b93c-9b1626621ad3
Read, Robert C.
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Moir, James W.B.
f6831b5f-5cfd-4c56-b3cd-6782f413a07f
February 2007
Rock, Jonathan D.
8e8fc55a-ebd8-4fcf-93e7-99b2909d34f0
Thomson, Melanie J.
a18b3a0f-1ec2-4928-b93c-9b1626621ad3
Read, Robert C.
b5caca7b-0063-438a-b703-7ecbb6fc2b51
Moir, James W.B.
f6831b5f-5cfd-4c56-b3cd-6782f413a07f
Rock, Jonathan D., Thomson, Melanie J., Read, Robert C. and Moir, James W.B.
(2007)
Regulation of denitrification genes in Neisseria meningitidis by nitric oxide and the repressor NsrR.
Journal of Bacteriology, 189 (3), .
(doi:10.1128/JB.01368-06).
Abstract
The human pathogen Neisseria meningitidis is capable of growth using the denitrification of nitrite to nitrous oxide under microaerobic conditions. This process is catalyzed by two reductases: nitrite reductase (encoded by aniA) and nitric oxide (NO) reductase (encoded by norB). Here, we show that in N. meningitidis MC58 norB is regulated by nitric oxide via the product of gene NMB0437 which encodes NsrR. NsrR is a repressor in the absence of NO, but norB expression is derepressed by NO in an NsrR-dependent manner. nsrR-deficient mutants grow by denitrification more rapidly than wild-type N. meningitidis, and this is coincident with the upregulation of both NO reductase and nitrite reductase even under aerobic conditions in the absence of nitrite or NO. The NsrR-dependent repression of aniA (unlike that of norB) is not lifted in the presence of NO. The role of NsrR in the control of expression of aniA is linked to the function of the anaerobic activator protein FNR: analysis of nsrR and fnr single and nsrR fnr double mutants carrying an aniA promoter lacZ fusion indicates that the role of NsrR is to prevent FNR-dependent aniA expression under aerobic conditions, indicating that FNR in N. meningitidis retains considerable activity aerobically.
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Accepted/In Press date: 13 November 2006
e-pub ahead of print date: 22 November 2006
Published date: February 2007
Keywords:
Aerobiosis, Anaerobiosis, Bacterial Outer Membrane Proteins, Bacterial Proteins, Blotting, Western, Gene Expression Regulation, Bacterial, Genes, Bacterial, Mutation, Neisseria meningitidis, Nitric Oxide, Nitric Oxide Donors, Nitrite Reductases, Nitrites, Nitrous Oxide, Oxidoreductases, Recombinant Fusion Proteins, Repressor Proteins, Journal Article, Research Support, Non-U.S. Gov't
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Local EPrints ID: 416317
URI: http://eprints.soton.ac.uk/id/eprint/416317
ISSN: 0021-9193
PURE UUID: 3c8e62a4-baba-467c-a4c3-851677fa7d8a
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Date deposited: 12 Dec 2017 17:30
Last modified: 16 Mar 2024 04:10
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Author:
Jonathan D. Rock
Author:
Melanie J. Thomson
Author:
James W.B. Moir
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