Fiche publication
Date publication
mai 2017
Journal
Nature communications
Auteurs
Membres identifiés du Cancéropôle Est :
Mme MESSADDEQ Nadia
,
Mme KOEBEL Pascale
Tous les auteurs :
Beilschmidt LK, Ollagnier de Choudens S, Fournier M, Sanakis I, Hograindleur MA, Clémancey M, Blondin G, Schmucker S, Eisenmann A, Weiss A, Koebel P, Messaddeq N, Puccio H, Martelli A
Lien Pubmed
Résumé
Mammalian A-type proteins, ISCA1 and ISCA2, are evolutionarily conserved proteins involved in iron-sulfur cluster (Fe-S) biogenesis. Recently, it was shown that ISCA1 and ISCA2 form a heterocomplex that is implicated in the maturation of mitochondrial FeS proteins. Here we report that mouse ISCA1 and ISCA2 are FeS-containing proteins that combine all features of Fe-S carrier proteins. We use biochemical, spectroscopic and in vivo approaches to demonstrate that despite forming a complex, ISCA1 and ISCA2 establish discrete interactions with components of the late Fe-S machinery. Surprisingly, knockdown experiments in mouse skeletal muscle and in primary cultures of neurons suggest that ISCA1, but not ISCA2, is required for mitochondrial FeS proteins biogenesis. Collectively, our data suggest that cellular processes with different requirements for ISCA1, ISCA2 and ISCA1-ISCA2 complex seem to exist.
Mots clés
Aconitate Hydratase, genetics, Animals, Binding Sites, Cloning, Molecular, Escherichia coli, genetics, Female, Gene Expression, Genetic Vectors, chemistry, Iron-Sulfur Proteins, genetics, Male, Mice, Mice, Inbred C57BL, Mitochondrial Proteins, genetics, Muscle, Skeletal, enzymology, Primary Cell Culture, Protein Binding, Protein Interaction Domains and Motifs, Protein Multimerization, Recombinant Proteins, genetics, Sensory Receptor Cells, cytology, Spectroscopy, Mossbauer
Référence
Nat Commun. 2017 May 11;8:15124
