PMID:12876288
| Citation |
Loiseau, L, Ollagnier-de-Choudens, S, Nachin, L, Fontecave, M and Barras, F (2003) Biogenesis of Fe-S cluster by the bacterial Suf system: SufS and SufE form a new type of cysteine desulfurase. J. Biol. Chem. 278:38352-9 |
|---|---|
| Abstract |
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. |
| Links |
PubMed Online version:10.1074/jbc.M305953200 |
| Keywords |
Alanine/chemistry; Bacterial Proteins/physiology; Carbon-Sulfur Lyases; Chromatography; Chromatography, Gel; Cysteine/pharmacology; Cytosol/metabolism; Dimerization; Dose-Response Relationship, Drug; Electrophoresis, Polyacrylamide Gel; Escherichia coli/metabolism; Immunoblotting; Iron-Sulfur Proteins/chemistry; Iron-Sulfur Proteins/physiology; Kinetics; Lyases/chemistry; Lyases/physiology; Models, Biological; Models, Chemical; Mutagenesis, Site-Directed; Pectobacterium chrysanthemi/metabolism; Plasmids/metabolism; Protein Binding; Selenocysteine/pharmacology; Subcellular Fractions; Time Factors; Two-Hybrid System Techniques |
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