The University of Southampton
University of Southampton Institutional Repository

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
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
0021-9193
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
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), 1138-1144. (doi:10.1128/JB.01368-06).

Record type: Article

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.

Full text not available from this repository.

More information

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

Identifiers

Local EPrints ID: 416317
URI: https://eprints.soton.ac.uk/id/eprint/416317
ISSN: 0021-9193
PURE UUID: 3c8e62a4-baba-467c-a4c3-851677fa7d8a
ORCID for Robert C. Read: ORCID iD orcid.org/0000-0002-4297-6728

Catalogue record

Date deposited: 12 Dec 2017 17:30
Last modified: 14 Mar 2019 01:36

Export record

Altmetrics

Contributors

Author: Jonathan D. Rock
Author: Melanie J. Thomson
Author: Robert C. Read ORCID iD
Author: James W.B. Moir

University divisions

Download statistics

Downloads from ePrints over the past year. Other digital versions may also be available to download e.g. from the publisher's website.

View more statistics

Atom RSS 1.0 RSS 2.0

Contact ePrints Soton: eprints@soton.ac.uk

ePrints Soton supports OAI 2.0 with a base URL of https://eprints.soton.ac.uk/cgi/oai2

This repository has been built using EPrints software, developed at the University of Southampton, but available to everyone to use.

We use cookies to ensure that we give you the best experience on our website. If you continue without changing your settings, we will assume that you are happy to receive cookies on the University of Southampton website.

×