Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 132, Issue 5, Pages 1506-+Publisher
AMER CHEMICAL SOC
DOI: 10.1021/ja909136h
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- Natural Sciences and Engineering Research Council of Canada (NSERC)
- Canadian Institutes of Health Research (CIHR)
- Canada Research Chairs Program
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The Escherichia coli NikR transcription factor is a Ni(II)-dependent repressor that regulates the production of a nickel ion transporter. The X-ray crystal structure of the Ni(II)-NikR-DNA bound complex revealed a K+-binding site positioned at the interface of the metal- and DNA-binding domains, but the significance of the potassium was unclear. Mutation of one of the K+ ligands impairs the affinity and specificity of DNA binding in the presence of either stoichiometric or excess Ni(II). Removal of K+ abrogates Ni(II)-responsive DNA binding completely while the addition of K+ restores this activity. Furthermore, the observed K+ dependence can be relieved by replacing the K+ ligand Asp34 with an arginine. These mutagenesis and cation exchange experiments reveal that K+ is a critical structural component for the activation of Ni(II)-responsive DNA binding by NikR.
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