Please use this identifier to cite or link to this item: http://hdl.handle.net/2440/69847
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Type: Journal article
Title: Novel bacterial MerR-like regulators: Their role in the response to carbonyl and nitrosative stress
Author: McEwan, A.
Djoko, K.
Chen, N.
Counago, R.
Kidd, S.
Potter, A.
Jennings, M.
Citation: Advances in Microbial Physiology, 2011; 58:1-22
Publisher: Academic Press Ltd
Issue Date: 2011
ISSN: 0065-2911
0065-2911
Statement of
Responsibility: 
Alastair G. McEwan, Karrera Y. Djoko, Nathan H. Chen, Rafael L.M. Couñago, Stephen P. Kidd, Adam J. Potter, Michael P. Jennings
Abstract: Recognition of the diversity of transcriptional regulators of the MerR family has increased considerably over the last decade and it has been established that not all MerR-like regulators are involved in metal ion recognition. A new type of MerR-like regulator was identified in Neisseria gonorrhoeae that is distinct from metal-binding MerR proteins. This novel transcription factor, the Neisseria merR-like regulator (NmlR) is related to a large and diverse group of MerR-like regulators. A common feature of the majority of the genes encoding the nmlR-related genes is that they predicted to control the expression of adhC, which encodes a glutathione-dependent alcohol dehydrogenase. The function of the NmlR regulon appears to be to defend the bacterial cell against carbonyl stress and in some cases nitrosative stress. A potential role for NmlR in bacterial pathogenesis has been identified in Neisseria gonorrhoeae and Streptococcus pneumoniae. Although it is not known how NmlR is activated it is suggested that conserved cysteine residues may be involved in thiol-based signaling.
Keywords: Cells, Cultured; Epithelial Cells; Animals; Humans; Neisseria gonorrhoeae; Streptococcus pneumoniae; Esterases; Aldehyde Oxidoreductases; Bacterial Proteins; DNA-Binding Proteins; Sequence Analysis, DNA; Signal Transduction; Transcription, Genetic; Gene Expression Regulation, Bacterial; Protein Conformation; Genes, Bacterial; Regulon; Stress, Physiological
Description: Chapter 1
Rights: Copyright © 2011 Elsevier Ltd. All rights reserved.
RMID: 0020111796
DOI: 10.1016/B978-0-12-381043-4.00001-5
Appears in Collections:Molecular and Biomedical Science publications

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