Ross R P, Claiborne A
Department of Biochemistry, Wake Forest University Medical Center, Winston Salem, NC 27157, USA.
FEMS Microbiol Lett. 1997 Jun 15;151(2):177-83. doi: 10.1111/j.1574-6968.1997.tb12567.x.
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.