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Transcriptional regulation by the dedicated nitric oxide sensor, NorR: a route towards NO detoxification

Bush, Matthew and Ghosh, Tamaswati and Tucker, Nicholas and Zhang, Xiaodong and Dixon, Ray (2011) Transcriptional regulation by the dedicated nitric oxide sensor, NorR: a route towards NO detoxification. Biochemical Society Transactions, 39 (1). pp. 289-293.

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Abstract

A flavorubredoxin and its associated oxidoreductase (encoded by norV and norW respectively) detoxify NO (nitric oxide) to form N2O (nitrous oxide) under anaerobic conditions in Escherichia coli. Transcription of the norVW genes is activated in response to NO by the σ54-dependent regulator and dedicated NO sensor, NorR, a member of the bacterial enhancer-binding protein family. In the absence of NO, the catalytic activity of the central ATPase domain of NorR is repressed by the N-terminal regulatory domain that contains a non-haem iron centre. Binding of NO to this centre results in the formation of a mononitrosyl iron species, enabling the activation of ATPase activity. Our studies suggest that the highly conserved GAFTGA loop in the ATPase domain, which engages with the alternative σ factor σ54 to activate transcription, is a target for intramolecular repression by the regulatory domain. Binding of NorR to three conserved enhancer sites upstream of the norVW promoter is essential for transcriptional activation and promotes the formation of a stable higher-order NorR nucleoprotein complex. We propose that enhancer-driven assembly of this oligomeric complex, in which NorR apparently forms a DNA-bound hexamer in the absence of NO, provides a 'poised' system for transcriptional activation that can respond rapidly to nitrosative stress.

Item type: Article
ID code: 31495
Keywords: escherichia coli proteins, gene expression regulation, models, nitric oxide, protein conformation, trans-activators, transcription, bacterial, molecular, genetic, Pharmacy and materia medica, Biochemistry
Subjects: Medicine > Pharmacy and materia medica
Department: Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences
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Depositing user: Pure Administrator
Date Deposited: 14 Jun 2011 15:24
Last modified: 27 Mar 2014 09:23
URI: http://strathprints.strath.ac.uk/id/eprint/31495

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