Open AccessEvidence for regulation of the NADH peroxidase gene ( npr ) from Enterococcus faecalis by OxyR
Author(s) -
Paul Ross R,
Claiborne Al
Publication year - 1997
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1997.tb12567.x
Subject(s) - enterococcus faecalis , escherichia coli , biology , polyclonal antibodies , gene , microbiology and biotechnology , peroxidase , promoter , antiserum , biochemistry , enterobacteriaceae , enzyme , gene expression , genetics , antibody
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.