Document Detail


Selenite and tellurite form mixed seleno- and tellurotrisulfides with CstR from Staphylococcus aureus.
MedLine Citation:
PMID:  23385876     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Staphylococcus aureus CstR (CsoR-like sulfur transferase repressor) is a member of the CsoR family of transition metal sensing metalloregulatory proteins. Unlike CsoR, CstR does not form a stable complex with transition metals but instead reacts with sulfite to form a mixture of di- and trisulfide species, CstR2(RS-SR') and CstR2(RS-S-SR')n)n=1 or 2, respectively. Here, we investigate if CstR performs similar chemistry with related chalcogen oxyanions selenite and tellurite. In this work we show by high resolution tandem mass spectrometry that CstR is readily modified by selenite (SeO3(2-)) or tellurite (TeO3(2-)) to form a mixture of intersubunit disulfides and selenotrisulfides or tellurotrisulfides, respectively, between Cys31 and Cys60'. Analogous studies with S. aureus CsoR reveals no reaction with selenite and minimal reaction with tellurite. All cross-linked forms of CstR exhibit reduced DNA binding affinity. We show that Cys31 initiates the reaction with sulfite through the formation of S-sulfocysteine (RS-SO3(2-)) and Cys60 is required to fully derivatize CstR to CstR2(RS-SR') and CstR2(RS-S-SR'). The modification of Cys31 also drives an allosteric switch that negatively regulates DNA binding while derivatization of Cys60 alone has no effect on DNA binding. These results highlight the differences between CstRs and CsoRs in chemical reactivity and metal ion selectivity and establish Cys31 as the functionally important cysteine residue in CstRs.
Authors:
Justin L Luebke; Randy J Arnold; David P Giedroc
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural    
Journal Detail:
Title:  Metallomics : integrated biometal science     Volume:  5     ISSN:  1756-591X     ISO Abbreviation:  Metallomics     Publication Date:  2013 Apr 
Date Detail:
Created Date:  2013-03-28     Completed Date:  2013-09-17     Revised Date:  2014-04-01    
Medline Journal Info:
Nlm Unique ID:  101478346     Medline TA:  Metallomics     Country:  England    
Other Details:
Languages:  eng     Pagination:  335-42     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Amino Acid Sequence
Bacterial Proteins / metabolism*
Chromatography, Liquid
Cross-Linking Reagents / pharmacology
Crystallography, X-Ray
Cysteine / metabolism
DNA, Bacterial / metabolism
Fluorescence Polarization
Kinetics
Molecular Sequence Data
Molecular Weight
Mutant Proteins / metabolism
Mycobacterium tuberculosis / drug effects,  metabolism
Peptides / chemistry,  metabolism
Protein Binding / drug effects
Sodium Selenite / metabolism*
Spectrometry, Mass, Electrospray Ionization
Staphylococcus aureus / drug effects,  metabolism*
Sulfides / metabolism*
Tandem Mass Spectrometry
Tellurium / metabolism*
Grant Support
ID/Acronym/Agency:
GM097225/GM/NIGMS NIH HHS; R01 GM097225/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Bacterial Proteins; 0/Cross-Linking Reagents; 0/DNA, Bacterial; 0/Mutant Proteins; 0/Peptides; 0/Sulfides; HIW548RQ3W/Sodium Selenite; IVA6SGP6QM/tellurous acid; K848JZ4886/Cysteine; NQA0O090ZJ/Tellurium
Comments/Corrections

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


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