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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.


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