Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/55319
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Type: Journal article
Title: NmlR of Neisseria gonorrhoeae : a novel redox responsive transcription factor from the MerR family
Author: Kidd, S.
Potter, A.
Apicella, M.
Jennings, M.
McEwan, A.
Citation: Molecular Microbiology, 2005; 57(6):1676-1689
Publisher: Blackwell Publishing Ltd
Issue Date: 2005
ISSN: 0950-382X
Statement of
Responsibility: 
Stephen P. Kidd, Adam J. Potter, Michael A. Apicella, Michael P. Jennings and Alastair G. McEwan
Abstract: A MerR-like regulator (NmlR –Neisseria merR-like Regulator) identified in the Neisseria gonorrhoeae genome lacks the conserved cysteines known to bind metal ions in characterized proteins of this family. Phylogenetic analysis indicates that NmlR defines a subfamily of MerR-like transcription factors with a distinctive pattern of conserved cysteines within their primary structure. NmlR regulates itself and three other genes in N. gonorrhoeae encoding a glutathione-dependent dehydrogenase (AdhC), a CPx-type ATPase (CopA) and a thioredoxin reductase (TrxB). An nmlR mutant lacked the ability to survive oxidative stress induced by diamide and cumene hydroperoxide. It also had > 50-fold lower NADH-S-nitrosoglutathione oxidoreductase activity consistent with a role for AdhC in protection against nitric oxide stress. The upstream sequences of the NmlR regulated genes contained typical MerR-like operator/promoter arrangements consisting of a dyad symmetry located between the −35 and −10 elements of the target genes. The NmlR target operator/promoters were cloned into a β-galactosidase reporter system and promoter activity was repressed by the introduction of NmlR in trans. Promoter activity was activated by NmlR in the presence of diamide. Under metal depleted conditions NmlR did not repress PAdhC (or PCopA) promoter activity, but this was reversed in the presence of Zn(II), indicating repression was Zn(II)-dependent. Analysis of mutated promoters lacking the dyad symmetry revealed constitutive promoter activity which was independent of NmlR. Gel shift assays further confirmed that NmlR bound to the target promoters possessing the dyad symmetry. Site-directed mutagenesis of the four NmlR cysteine residues revealed that they were essential for activation of gene expression by NmlR
Description: Journal compilation © 2005 Blackwell Publishing
RMID: 0020092900
DOI: 10.1111/j.1365-2958.2005.04773.x
Appears in Collections:Molecular and Biomedical Science publications

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