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Article

Purification and functional characterization of MerD. A coregulator of the mercury resistance operon in gram-negative bacteria.

The Journal of biological chemistry - 5 Oct 1991

Mukhopadhyay D, Yu H R, Nucifora G, Misra T K

Abstract excerpt

Mercury resistance operons (mer) from transposons Tn21, Tn501, and plasmid pDU1358 are highly homologous and inducible with Hg2+. The regulatory gene merR is transcribed from one promoter, which is divergently oriented from the promoter for the other mer genes. MerR, the product of the regulatory gene, negatively regulates its own expression as well as the expression of the other genes. MerR activates...

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PMID: 1917975

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Purification and functional characterization of MerD. A coregulator of the mercury resistance operon in gram-negative bacteria.PMID 1917975Read ↗

Construction and characterization of a mercury-independent MerR activator (MerRAC): transcriptional activation in the absence of Hg(II) is accompanied by DNA distortion.Semantic proximity Read ↗

Site-specific insertion and deletion mutants in the mer promoter-operator region of Tn501; the nineteen base-pair spacer is essential for normal induction of the promoter by MerR.Semantic proximity Read ↗

Cd(II)-responsive and constitutive mutants implicate a novel domain in MerR.Semantic proximity Read ↗

Construction of a synthetic gene for the metalloregulatory protein MerR and analysis of regionally mutated proteins for transcriptional regulation.Semantic proximity Read ↗

Selection and characterization of mercury-independent activation mutants of the Tn501 transcriptional regulator, MerR.Semantic proximity Read ↗

Mutations in the alpha and sigma-70 subunits of RNA polymerase affect expression of the mer operon.Semantic proximity Read ↗

NmlR of Neisseria gonorrhoeae: a novel redox responsive transcription factor from the MerR family.Semantic proximity Read ↗

In vivo DNA-protein interactions at the divergent mercury resistance (mer) promoters. II. Repressor/activator (MerR)-RNA polymerase interaction with merOP mutants.Semantic proximity Read ↗

The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer.Semantic proximity Read ↗

Deletion mutant analysis of the Staphylococcus aureus plasmid pI258 mercury-resistance determinant.Semantic proximity Read ↗

Overexpression of MerT, the mercuric ion transport protein of transposon Tn501, and genetic selection of mercury hypersensitivity mutations.Semantic proximity Read ↗

Adaptation to mercury stress by nitrogen-fixing bacteria is driven by horizontal gene transfer and enhanced gene expression of the Mer operonSemantic proximity Read ↗

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