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Phase Variation of Ag43 is Independent of the Oxidation State of OxyR may end with a question mark. Please enter as plain text. If you have a subtitle, it should be preceded with a colon [:]. Use capitals only for the first word and for proper nouns.

Wallecha, A., Correnti, J., Munster, V. and van der Woude, M. (2002) Phase Variation of Ag43 is Independent of the Oxidation State of OxyR may end with a question mark. Please enter as plain text. If you have a subtitle, it should be preceded with a colon [:]. Use capitals only for the first word and for proper nouns. Journal of Bacteriology, 185 (7). pp. 2203-2209. ISSN 0021-9193

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Abstract

OxyR is a DNA binding protein that differentially regulates a cell's response to hydrogen peroxide-mediated oxidative stress. We previously reported that the reduced form of OxyR is sufficient for repression of transcription of agn43 from unmethylated template DNA, which is essential for deoxyadenosine methylase (Dam)- and OxyR-dependent phase variation of agn43. Here we provide evidence that the oxidized form of OxyR [OxyR(ox)] also represses agn43 transcription. In vivo, we found that exogenous addition of hydrogen peroxide, sufficient to oxidize OxyR, did not affect the expression of agn43. OxyR(ox) repressed in vitro transcription but only from an unmethylated agn43 template. The -10 sequence of the promoter and three Dam target sequences were protected in an in vitro DNase I footprint assay by OxyR(ox). Furthermore, OxyR(ox) bound to the agn43 regulatory region DNA with an affinity similar to that for the regulatory regions of katG and oxyS, which are activated by OxyR(ox), indicating that binding at agn43 can occur at biologically relevant concentrations. OxyR-dependent regulation of Ag43 expression is therefore unusual in firstly that OxyR binding at agn43 is dependent on the methylation state of Dam target sequences in its binding site and secondly that OxyR-dependent repression appears to be independent of hydrogen-peroxide mediated oxidative stress and the oxidation state of OxyR.

Item Type: Article
Academic Units: The University of York > Hull York Medical School (York)
Depositing User: York RAE Import
Date Deposited: 09 Feb 2009 12:50
Last Modified: 09 Feb 2009 12:50
Published Version: http://dx.doi.org/10.1128/JB.185.7.2203-2209.2003
Status: Published
Publisher: American Society for Microbiology
Identification Number: 10.1128/JB.185.7.2203-2209.2003
URI: http://eprints.whiterose.ac.uk/id/eprint/7667

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