Document Detail


SufE transfers sulfur from SufS to SufB for iron-sulfur cluster assembly.
MedLine Citation:
PMID:  17350958     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Iron-sulfur (Fe-S) clusters are key metal cofactors of metabolic, regulatory, and stress response proteins in most organisms. The unique properties of these clusters make them susceptible to disruption by iron starvation or oxidative stress. Both iron and sulfur can be perturbed under stress conditions, leading to Fe-S cluster defects. Bacteria and higher plants contain a specialized system for Fe-S cluster biosynthesis under stress, namely the Suf pathway. In Escherichia coli the Suf pathway consists of six proteins with functions that are only partially characterized. Here we describe how the SufS and SufE proteins interact with the SufBCD protein complex to facilitate sulfur liberation from cysteine and donation for Fe-S cluster assembly. It was previously shown that the cysteine desulfurase SufS donates sulfur to the sulfur transfer protein SufE. We have found here that SufE in turn interacts with the SufB protein for sulfur transfer to that protein. The interaction occurs only if SufC is present. Furthermore, SufB can act as a site for Fe-S cluster assembly in the Suf system. This provides the first evidence of a novel site for Fe-S cluster assembly in the SufBCD complex.
Authors:
Gunhild Layer; S Aparna Gaddam; Carla N Ayala-Castro; Sandrine Ollagnier-de Choudens; David Lascoux; Marc Fontecave; F Wayne Outten
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2007-03-09
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  282     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2007 May 
Date Detail:
Created Date:  2007-04-30     Completed Date:  2007-06-14     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  13342-50     Citation Subset:  IM    
Affiliation:
Laboratoire de Chimie et Biologie des Métaux, iRTSV/LCBM, Commissariat a l'Energie Atomique/CNRS/Universite Joseph Fourier, CEA-Grenoble, UMR 5249, 17 Avenue des Martyrs, 38054 Grenoble Cedex 09, France.
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MeSH Terms
Descriptor/Qualifier:
Biological Transport, Active / physiology
Carrier Proteins / genetics,  metabolism*
Escherichia coli / genetics,  metabolism*
Escherichia coli Proteins / genetics,  metabolism*
Iron / metabolism*
Lyases / genetics,  metabolism*
Models, Molecular
Multiprotein Complexes / genetics,  metabolism
Oxidative Stress / physiology
Sulfur / metabolism*
Chemical
Reg. No./Substance:
0/Carrier Proteins; 0/Escherichia coli Proteins; 0/Multiprotein Complexes; 0/Suf E protein, E coli; 0/SufB protein, E coli; 7439-89-6/Iron; 7704-34-9/Sulfur; EC 4.-/Lyases; EC 4.4.1.16/selenocysteine lyase

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


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