SufC: an unorthodox cytoplasmic ABC/ATPase required for [Fe-S] biogenesis under oxidative stress
Open Access
- 3 February 2003
- journal article
- research article
- Published by Springer Nature in The EMBO Journal
- Vol. 22 (3) , 427-437
- https://doi.org/10.1093/emboj/cdg061
Abstract
Proteins containing [Fe—S] clusters perform essential functions in all domains of life. Previously, we identified the sufABCDSE operon as being necessary for virulence of the plant pathogen Erwinia chrysanthemi . In addition, we collected preliminary evidence that the sufABCDSE operon might be involved in the assembly of [Fe—S] clusters. Of particular interest are the sufB, sufC and sufD genes, which are conserved among Eubacteria, Archaea, plants and parasites. The present study establishes SufC as an unorthodox ATPase of the ABC superfamily that is located in the cytosol, wherein it interacts with both SufB and SufD. Moreover, under oxidative stress conditions, SufC was found to be necessary for the activity of enzymes containing oxygen‐labile [Fe—S] clusters, but dispensable for glutamate synthase, which contains an oxidatively stable [Fe—S] cluster. Lastly, we have shown SufBCD to be essential for iron acquisition via chrysobactin, a siderophore of major importance in virulence. We discuss a model wherein the SufBCD proteins contribute to bacterial pathogenicity via their role in the assembly of [Fe—S] clusters under oxidative stress and iron limitation.Keywords
This publication has 52 references indexed in Scilit:
- SufC hydrolyzes ATP and interacts with SufB from Thermotoga maritimaFEBS Letters, 2002
- The PDZ domain of OutC and the N-terminal region of OutD determine the secretion specificity of the type II out pathway of Erwinia chrysanthemiJournal of Molecular Biology, 2001
- Crystal structure of the SMC head domain: an ABC ATPase with 900 residues antiparallel coiled-coil insertedJournal of Molecular Biology, 2001
- Composite Active Site of an ABC ATPaseMolecular Cell, 2001
- Structural Biology of Rad50 ATPaseCell, 2000
- Saccharomyces cerevisiae ISU1 and ISU2: members of a well-conserved gene family for iron-sulfur cluster assemblyJournal of Molecular Biology, 1999
- ABC-ATPases, adaptable energy generators fuelling transmembrane movement of a variety of molecules in organisms from bacteria to humansJournal of Molecular Biology, 1999
- Inventory, assembly and analysis of Bacillus subtilis ABC transport systemsJournal of Molecular Biology, 1999
- Iron—sulfur proteins: new roles for old clustersCurrent Opinion in Chemical Biology, 1998
- Activation of SoxR-dependent Transcription in Vitro by Noncatalytic or NifS-mediated Assembly of [2Fe-2S[ Clusters into Apo-SoxRPublished by Elsevier ,1996