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http://hdl.handle.net/2445/67192
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DC Field | Value | Language |
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dc.contributor.author | Parent, Aubérie | - |
dc.contributor.author | Elduque Busquets, Xavier | - |
dc.contributor.author | Cornu, David | - |
dc.contributor.author | Belot, Laura | - |
dc.contributor.author | Le Caer, Jean-Pierre | - |
dc.contributor.author | Grandas Sagarra, Anna | - |
dc.contributor.author | Toledano, Michel B. | - |
dc.contributor.author | D'Autréaux, Benoit | - |
dc.date.accessioned | 2015-10-08T10:35:25Z | - |
dc.date.available | 2015-10-08T10:35:25Z | - |
dc.date.issued | 2014-01-19 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | http://hdl.handle.net/2445/67192 | - |
dc.description.abstract | Friedreich's ataxia is a severe neurodegenerative disease caused by the decreased expression of frataxin, a mitochondrial protein that stimulates iron <br>sulfur (Fe-S) cluster biogenesis. In mammals, the primary steps of Fe-S cluster assembly are performed by the NFS1 <br>ISD11 <br>ISCU complex via the formation of a persulfide intermediate on NFS1. Here we show that frataxin modulates the reactivity of NFS1 persulfide with thiols. We use maleimide-peptide com- pounds along with mass spectrometry to probe cysteine-persulfide in NFS1 and ISCU. Our data reveal that in the presence of ISCU, frataxin enhances the rate of two similar reactions on NFS1 persulfide: sulfur transfer to ISCU leading to the accumulation of a persulfide on the cysteine C104 of ISCU, and sulfur transfer to small thiols such as DTT, L-cysteine and GSH leading to persulfuration of these thiols and ultimately sulfide release. These data raise important questions on the physiological mechanism of Fe-S cluster assembly and point to a unique function of frataxin as an enhancer of sulfur transfer within the NFS1 <br>ISD11 <br>ISCU complex. | - |
dc.format.extent | 12 p. | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | - |
dc.publisher | Nature Publishing Group | - |
dc.relation.isformatof | Versió postprint del document publicat a: http://dx.doi.org/10.1038/ncomms6686 | - |
dc.relation.ispartof | Nature Communications, 2014, vol. 6 | - |
dc.relation.uri | http://dx.doi.org/10.1038/ncomms6686 | - |
dc.rights | (c) Parent et al., 2014 | - |
dc.source | Articles publicats en revistes (Química Inorgànica i Orgànica) | - |
dc.subject.classification | Bioquímica | - |
dc.subject.classification | Malalties neurodegeneratives | - |
dc.subject.classification | Proteïnes | - |
dc.subject.other | Biochemistry | - |
dc.subject.other | Neurodegenerative Diseases | - |
dc.subject.other | Proteins | - |
dc.title | Mammalian frataxin directly enhances sulfur transfer of NFS1 persulfide to both ISCU and free thiols | - |
dc.type | info:eu-repo/semantics/article | - |
dc.type | info:eu-repo/semantics/acceptedVersion | - |
dc.identifier.idgrec | 652080 | - |
dc.date.updated | 2015-10-08T10:35:25Z | - |
dc.rights.accessRights | info:eu-repo/semantics/openAccess | - |
dc.identifier.pmid | 25597503 | - |
Appears in Collections: | Articles publicats en revistes (Química Inorgànica i Orgànica) |
Files in This Item:
File | Description | Size | Format | |
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652080.pdf | 1.42 MB | Adobe PDF | View/Open |
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