期刊
MITOCHONDRION
卷 12, 期 5, 页码 539-549出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.mito.2012.07.103
关键词
Cysteine desulfurase; Nfs1p.Isd11p complex; Persulfide; Fe-S clusters; Aconitase; Yeast
资金
- National Institutes of Health from NIGMS [GM087965]
- NIA [AG030504]
- American Heart Association [09GRNT2260364]
- [R37DK053953]
Cysteine desulfurases generate a covalent persulfide intermediate from cysteine, and this activated form of sulfur is essential for the synthesis of iron-sulfur (Fe-S) clusters. In yeast mitochondria, there is a complete machinery for Fe-S cluster synthesis, including a cysteine desulfurase, Nfs1p. Here we show that following supplementation of isolated mitochondria with [S-35]cysteine, a radiolabeled persulfide could be detected on Nfs1p. The persulfide persisted under conditions that did not permit Fe-S cluster formation, such as nucleotide and/or iron depletion of mitochondria. By contrast, under permissive conditions, the radiolabeled Nfs1p persulfide was greatly reduced and radiolabeled aconitase was formed, indicating transfer of persulfide to downstream Fe-S cluster recipients. Nfs1p in mitochondria was found to be relatively more resistant to inactivation by N-ethylmaleimide (NEM) as compared with a prokaryotic cysteine desulfurase. Mitochondria treated with NEM (1 mM) formed the persulfide on Nfs1p but failed to generate Fe-S clusters on aconitase, likely due to inactivation of downstream recipient(s) of the Nfs1p persulfide. Thus the Nfsl p-bound persulfide as described here represents a precursor en route to Fe-S cluster synthesis in mitochondria. (C) 2012 Elsevier B.V. and Mitochondria Research Society. All rights reserved.
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