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Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR.

作者信息

Ross R P, Claiborne A

机构信息

Department of Biochemistry, Wake Forest University Medical Center, Winston Salem, NC 27157, USA.

出版信息

FEMS Microbiol Lett. 1997 Jun 15;151(2):177-83. doi: 10.1111/j.1574-6968.1997.tb12567.x.

Abstract

We report that the purified Escherichia coli OxyR protein can bind specifically upstream of the gene encoding NADH peroxidase (npr) from Enterococcus faecalis 10C1, to a site located some 144 bp from the promoter. A 34 kDa protein has been identified in crude extracts of E. faecalis that cross-reacts with polyclonal antisera to purified OxyR from E. coli and a protein(s) present in these extracts retards npr DNA fragments in gel shift assays. Taken together with the results of sequence analyses, these observations suggest that enterococcal npr is regulated by OxyR.

摘要

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