Evidence for regulation of the NADH peroxidase gene (npr) from Enterococcus faecalis by OxyR.
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.
Ross
R P
RP
Department of Biochemistry, Wake Forest University Medical Center, Winston Salem, NC 27157, USA. pross@dpc.teagasc.ie
Claiborne
A
A
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000502:physiology*; D001483:Base Sequence; D004268:DNA-Binding Proteins; D013293:Enterococcus faecalis / Q000235:genetics*; D029968:Escherichia coli Proteins; D015971:Gene Expression Regulation, Enzymologic; D005798:Genes, Bacterial; D008969:Molecular Sequence Data; D010544:Peroxidases / Q000235:genetics*; D011401:Promoter Regions, Genetic; D012097:Repressor Proteins / Q000502:physiology*; D014157:Transcription Factors / Q000502:physiology*
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D029968:Escherichia coli Proteins; D012097:Repressor Proteins; D014157:Transcription Factors; C499299:oxyR protein, E coli; D010544:Peroxidases; C021845:NAD+ peroxidase