NDLI: Role of bound Zn(II) in the CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor.

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Role of bound Zn(II) in the CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Rosen, Barry P. Stemmler, Timothy L. Kondapalli, Kalyan C. Kandegedara, Ashoka Thiyagarajan, Saravanamuthu
Description	Author Affiliation: Kandegedara A ( Department of Biochemistry and Molecular Biology, Wayne State University, School of Medicine, Detroit, Michigan 48201, USA.)
Abstract	The Staphylococcus aureus plasmid pI258 cadCA operon encodes a P-type ATPase, CadA, that confers resistance to Cd(II)/Pb(II)/Zn(II). Expression is regulated by CadC, a homodimeric repressor that dissociates from the cad operator/promoter upon binding of Cd(II), Pb(II), or Zn(II). CadC is a member of the ArsR/SmtB family of metalloregulatory proteins. The crystal structure of CadC shows two types of metal binding sites, termed Site 1 and Site 2, and the homodimer has two of each. Site 1 is the physiological inducer binding site. The two Site 2 metal binding sites are formed at the dimerization interface. Site 2 is not regulatory in CadC but is regulatory in the homologue SmtB. Here the role of each site was investigated by mutagenesis. Both sites bind either Cd(II) or Zn(II). However, Site 1 has higher affinity for Cd(II) over Zn(II), and Site 2 prefers Zn(II) over Cd(II). Site 2 is not required for either derepression or dimerization. The crystal structure of the wild type with bound Zn(II) and of a mutant lacking Site 2 was compared with the SmtB structure with and without bound Zn(II). We propose that an arginine residue allows for Zn(II) regulation in SmtB and, conversely, a glycine results in a lack of regulation by Zn(II) in CadC. We propose that a glycine residue was ancestral whether the repressor binds Zn(II) at a Site 2 like CadC or has no Site 2 like the paralogous ArsR and implies that acquisition of regulatory ability in SmtB was a more recent evolutionary event.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	22
Volume Number	284
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2009-05-29
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Bacterial Proteins Metabolism Metals, Heavy Repressor Proteins Staphylococcus Aureus Chemistry Binding Sites Cadmium Crystallography, X-Ray DNA-Binding Proteins Kinetics Mass Spectrometry Mutant Proteins Mutation Genetics Protein Multimerization Protein Structure, Secondary Zinc Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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