NDLI: Characterization of a metalloregulatory bismuth(III) site in Staphylococcus aureus pI258 CadC repressor

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Characterization of a metalloregulatory bismuth(III) site in Staphylococcus aureus pI258 CadC repressor

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Characterization of a metalloregulatory bismuth(III) site in Staphylococcus aureus pI258 CadC repressor

Content Provider	Springer Nature Link
Author	Busenlehner, Laura S. Apuy, Julius L. Giedroc, David P.
Copyright Year	2002
Abstract	Staphylococcus aureus pI258 CadC is a metal sensor protein that regulates the expression of the cad operon which encodes metal ion resistance proteins involved in the efficient efflux of Cd(II), Pb(II), Zn(II) and, according to one report , Bi(III) ions. In this paper, direct evidence is presented that Bi(III) binds to CadC and negatively regulates cad operator/promoter (O/P) binding. Optical absorption spectroscopy reveals that dimeric CadC binds ∼0.8 mol equivalents of Bi(III) per CadC monomer to form a coordination complex characterized by three S–→Bi(III) ligand-to-metal charge transfer transitions, with the longest wavelength absorption band centered at 415 nm (ε415=4000 MBi –1 cm–1). UV-Vis absorption spectra of wild-type and mutant Cys→Gly (Ser) substitution CadC mutants compared to [Bi(DTT)2], [Bi(GSH)3] and [Bi(NAC)]3 model complexes reveal that Cys7, Cys11, Cys60 and Cys58 directly coordinate Bi(III) in a tetrathiolate coordination complex. The apparent affinity derived from a Bi(III)-displacement optical titration with Cd(II) is estimated to be K Bi≤1012 M–1. Apo-CadC binds with high affinity [K a=1.1(±0.3)×109 M–1; 0.40 M NaCl, pH 7.0, 25 °C] to a 5′-fluorescein-labeled cad O/P oligonucleotide ,while the binding of one molar equivalent of Bi(III) per CadC monomer (Bi1-CadC) reduces the affinity by ∼170-fold. Strikingly, Bi(III)-responsive negative regulation of cad O/P binding is abrogated for Bi1-C60G CadC and severely disrupted in Bi1-C7G CadC, whose relative affinity is reduced only 10-fold. The mechanism of Bi(III)-responsive metalloregulation is discussed, based on the findings presented here. Electronic supplementary material to this paper can be obtained by using the Springer Link server located at http://dx.doi.org/10.1007/s00775-001-0336-9.
Starting Page	551
Ending Page	559
Page Count	9
File Format	PDF
ISSN	09498257
Journal	JBIC Journal of Biological Inorganic Chemistry
Volume Number	7
Issue Number	4-5
e-ISSN	14321327
Language	English
Publisher	Springer-Verlag
Publisher Date	2002-02-08
Publisher Place	Berlin, Heidelberg
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Biochemistry Microbiology
Content Type	Text
Resource Type	Article
Subject	Biochemistry Inorganic Chemistry

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