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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
40
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pubmed:dateCreated |
2003-9-29
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pubmed:abstractText |
Biosynthesis of iron-sulfur clusters (Fe-S) depends on multiprotein systems. Recently, we described the SUF system of Escherichia coli and Erwinia chrysanthemi as being important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet. Here we demonstrate that: (i) SufE and SufS are both cystosolic as all members of the SUF system; (ii) SufE is a homodimeric protein; (iii) SufE forms a complex with SufS as shown by the yeast two-hybrid system and by affinity chromatography; (iv) binding of SufE to SufS is responsible for a 50-fold stimulation of the cysteine desulfurase activity of SufS. This is the first example of a two-component cysteine desulfurase enzyme.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
3
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pubmed:volume |
278
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
38352-9
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12876288-Alanine,
pubmed-meshheading:12876288-Bacterial Proteins,
pubmed-meshheading:12876288-Carbon-Sulfur Lyases,
pubmed-meshheading:12876288-Chromatography,
pubmed-meshheading:12876288-Chromatography, Gel,
pubmed-meshheading:12876288-Cysteine,
pubmed-meshheading:12876288-Cytosol,
pubmed-meshheading:12876288-Dimerization,
pubmed-meshheading:12876288-Dose-Response Relationship, Drug,
pubmed-meshheading:12876288-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:12876288-Escherichia coli,
pubmed-meshheading:12876288-Immunoblotting,
pubmed-meshheading:12876288-Iron-Sulfur Proteins,
pubmed-meshheading:12876288-Kinetics,
pubmed-meshheading:12876288-Lyases,
pubmed-meshheading:12876288-Models, Biological,
pubmed-meshheading:12876288-Models, Chemical,
pubmed-meshheading:12876288-Mutagenesis, Site-Directed,
pubmed-meshheading:12876288-Pectobacterium chrysanthemi,
pubmed-meshheading:12876288-Plasmids,
pubmed-meshheading:12876288-Protein Binding,
pubmed-meshheading:12876288-Selenocysteine,
pubmed-meshheading:12876288-Subcellular Fractions,
pubmed-meshheading:12876288-Time Factors,
pubmed-meshheading:12876288-Two-Hybrid System Techniques
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pubmed:year |
2003
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pubmed:articleTitle |
Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase.
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pubmed:affiliation |
LCB-CNRS, IBSM, 31 Chemin Joseph Aiguier, 13402 Marseille 20, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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