Document Detail


The soft metal ion binding sites in the Staphylococcus aureus pI258 CadC Cd(II)/Pb(II)/Zn(II)-responsive repressor are formed between subunits of the homodimer.
MedLine Citation:
PMID:  12176999     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
The Staphylococcus aureus plasmid pI258 CadC is a homodimeric repressor that binds Cd(II), Pb(II), and Zn(II) and regulates expression of the cadAC operon. CadC binds two Cd(II) ions per dimer, with a tetrathiolate binding site composed of residues Cys(7), Cys(11), Cys(58), and Cys(60). It is not known whether each site consists of residues from a single monomer or from residues contributed by both subunits. To examine whether Cys(7) and Cys(11) are spatially proximate to Cys(58) and Cys(60) of the same subunit or of the other subunit, homodimers with the same cysteine mutation in each subunit and heterodimers containing different cysteine mutations in the two subunits were reacted with 4,6-bis(bromomethyl)-3,7-dimethyl-1,5-diazabicyclo[3.3.0]octa-3,6-diene-2,8-dione, which cross-links thiol groups that are within 3-6 A of each other. Cys(7) or Cys(11) cross-linked only with Cys(58) or Cys(60) on the other subunit. The data demonstrate that Cys(7) and Cys(11) from one monomer are within 3-6 A of either Cys(58) or Cys(60) in the other monomer. The results of this study strongly indicate that each of the two Cd(II) binding sites in the CadC homodimer is composed of Cys(7) and Cys(11) from one monomer and Cys(58) and Cys(60) from the other monomer.
Authors:
Marco D Wong; Yung-Feng Lin; Barry P Rosen
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, P.H.S.     Date:  2002-08-09
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  277     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2002 Oct 
Date Detail:
Created Date:  2002-10-25     Completed Date:  2002-12-09     Revised Date:  2007-11-14    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  40930-6     Citation Subset:  IM    
Affiliation:
Department of Biochemistry and Molecular Biology, School of Medicine, Wayne State University, 540 E Canfield Avenue, Detroit, MI 48201, USA.
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / chemistry,  genetics,  metabolism*
Binding Sites
Blotting, Western
Dimerization
Metals, Heavy / metabolism*
Molecular Sequence Data
Mutagenesis, Site-Directed
Repressor Proteins / chemistry,  genetics,  metabolism*
Sequence Homology, Amino Acid
Staphylococcus aureus / metabolism*
Grant Support
ID/Acronym/Agency:
AI 45428/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/CadC protein, Bacteria; 0/Metals, Heavy; 0/Repressor Proteins

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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