PMID:15901727
| Citation |
Loiseau, L, Ollagnier-de Choudens, S, Lascoux, D, Forest, E, Fontecave, M and Barras, F (2005) Analysis of the heteromeric CsdA-CsdE cysteine desulfurase, assisting Fe-S cluster biogenesis in Escherichia coli. J. Biol. Chem. 280:26760-9 |
|---|---|
| Abstract |
Biogenesis of iron-sulfur (Fe-S) cluster-containing proteins relies on assistance of complex machineries. To date three systems, NIF, ISC, and SUF, were reported to allow maturation of Fe-S proteins. Here we report that the csdA-csdE (formally ygdK) genes of Escherichia coli constitute a sulfur-generating system referred to as CSD which also contributes to Fe-S biogenesis in vivo. This conclusion was reached by applying a thorough combination of both in vivo and in vitro strategies and techniques. Yeast two-hybrid analysis allowed us to show that CsdA and CsdE interact. Enzymology analysis showed that CsdA cysteine desulfurase activity is increased 2-fold in the presence of CsdE. Mass spectrometry analysis and site-directed mutagenesis showed that residue Cys-61 from CsdE acted as an acceptor site for sulfur provided by cysteine desulfurase activity of CsdA. Genetic investigations revealed that the csdA-csdE genes could act as multicopy suppressors of iscS mutation. Moreover, both in vitro and in vivo investigations pointed to a specific connection between the CSD system and quinolinate synthetase NadA. |
| Links |
PubMed Online version:10.1074/jbc.M504067200 |
| Keywords |
Binding Sites; Carbon-Sulfur Lyases/chemistry; Carbon-Sulfur Lyases/genetics; Carbon-Sulfur Lyases/metabolism; Dimerization; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Iron-Sulfur Proteins/biosynthesis; Kinetics; Multienzyme Complexes; Mutagenesis, Site-Directed; Protein Binding; Two-Hybrid System Techniques |
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