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Science 23 February 1990:
Vol. 247. no. 4945, pp. 946 - 948
DOI: 10.1126/science.2305262
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Articles

Science, Vol 247, Issue 4945, 946-948
Copyright © 1990 by American Association for the Advancement of Science

articles

The MerR metalloregulatory protein binds mercuric ion as a tricoordinate, metal-bridged dimer

JD Helmann, BT Ballard, and CT Walsh

Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.

Bacterial MerR proteins are dimeric DNA-binding proteins that mediate the Hg(II)-dependent induction of mercury resistance operons. Site-directed mutagenesis of the Bacillus sp. RC607 MerR protein reveals that three of four Cys residues per monomer are required for Hg(II) binding at the single high-affinity binding site. Inactive mutant homodimers can exchange subunits to form heterodimers active for Hg(II) binding. Studies of a heterodimer retaining only three of eight cysteine residues per dimer reveal that Cys79 in one subunit and Cys114 and Cys123 in the second subunit are necessary and sufficient for high-affinity Hg(II) binding in an asymmetric, subunit bridging coordination complex.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Hg(II) sequestration and protection by the MerR metal-binding domain (MBD)..
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The TetR Family of Transcriptional Repressors.
J. L. Ramos, M. Martinez-Bueno, A. J. Molina-Henares, W. Teran, K. Watanabe, X. Zhang, M. T. Gallegos, R. Brennan, and R. Tobes (2005)
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Engineered Single-Chain, Antiparallel, Coiled Coil Mimics the MerR Metal Binding Site.
L. Song, J. Caguiat, Z. Li, J. Shokes, R. A. Scott, L. Olliff, and A. O. Summers (2004)
J. Bacteriol. 186, 1861-1868
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Molecular Basis of Metal-Ion Selectivity and Zeptomolar Sensitivity by CueR.
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Enhanced Mercury Biosorption by Bacterial Cells with Surface-Displayed MerR.
W. Bae, C. H. Wu, J. Kostal, A. Mulchandani, and W. Chen (2003)
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Transposition of DEH, a Broad-Host-Range Transposon Flanked by ISPpu12, in Pseudomonas putida Is Associated with Genomic Rearrangements and Dehalogenase Gene Silencing.
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Osmotic regulation of the Streptomyces lividans thiostrepton-inducible promoter, ptipA.
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Mercury Resistance in Bacillus cereus RC607: Transcriptional Organization and Two New Open Reading Frames.
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Cd(II)-Responsive and Constitutive Mutants Implicate a Novel Domain in MerR.
J. J. Caguiat, A. L. Watson, and A. O. Summers (1999)
J. Bacteriol. 181, 3462-3471
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Identification of a Novel Transcription Regulator from Proteus mirabilis, PMTR, Revealed a Possible Role of YJAI Protein in Balancing Zinc in Escherichia coli.
M. Noll, K. Petrukhin, and S. Lutsenko (1998)
J. Biol. Chem. 273, 21393-21401
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Binuclear [2Fe-2S] Clusters in the Escherichia coli SoxR Protein and Role of the Metal Centers in Transcription.
E. Hidalgo, J. M. Bollinger Jr., T. M. Bradley, C. T. Walsh, and B. Demple (1995)
J. Biol. Chem. 270, 20908-20914
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Mercury-199 NMR of the metal receptor site in MerR and its protein-DNA complex.
L. Utschig, J. Bryson, and T. O'Halloran (1995)
Science 268, 380-385
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Transition metals in control of gene expression.
T. O'Halloran (1993)
Science 261, 715-725
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