PMID: 2492496Jan 1, 1989Paper

Homologous metalloregulatory proteins from both gram-positive and gram-negative bacteria control transcription of mercury resistance operons

Journal of Bacteriology
J D HelmannC T Walsh

Abstract

We report the overexpression, purification, and properties of the regulatory protein, MerR, for a chromosomally encoded mercury resistance determinant from Bacillus strain RC607. This protein is similar in sequence to the metalloregulatory proteins encoded by gram-negative resistance determinants found on transposons Tn21 and Tn501 and to a predicted gene product of a Staphylococcus aureus resistance determinant. In vitro DNA-binding and transcription experiments were used to demonstrate those purified Bacillus MerR protein controls transcription from a promoter-operator site similar in sequence to that found in the transposon resistance determinants. The Bacillus MerR protein bound in vitro to its promoter-operator region in both the presence and absence of mercuric ion and functioned as a negative and positive regulator of transcription. The MerR protein bound less tightly to its operator region (ca. 50- to 100-fold) in the presence of mercuric ion; this reduced affinity was largely accounted for by an increased rate of dissociation of the MerR protein from the DNA. Despite this reduced DNA-binding affinity, genetic and biochemical evidence support a model in which the MerR protein-mercuric ion complex is a positive regulator...Continue Reading

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Citations

Oct 1, 1995·European Journal of Biochemistry·J A BotellaR Ruiz-Vázquez
Apr 1, 1997·FEMS Microbiology Reviews·A M OsbornD A Ritchie
Oct 1, 1990·Molecular Microbiology·H Hennecke
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Jun 7, 2006·BMC Microbiology·E A PerminaM S Gelfand
Dec 8, 1998·Biochemistry·Q ZengA O Summers

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