{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Beilschmidt LK"],"funding":["European Research Council"],"pagination":["15124"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC5437272"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["8"],"pubmed_abstract":["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 Fe<sub>4</sub>S<sub>4</sub> proteins. Here we report that mouse ISCA1 and ISCA2 are Fe<sub>2</sub>S<sub>2</sub>-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 Fe<sub>"],"journal":["Nature communications"],"pubmed_title":["ISCA1 is essential for mitochondrial Fe<sub>4</sub>S<sub>4</sub> biogenesis in vivo."],"pmcid":["PMC5437272"],"funding_grant_id":["206634"],"pubmed_authors":["Martelli A","Koebel P","Fournier M","Weiss A","Clemancey M","Beilschmidt LK","Sanakis I","Puccio H","Hograindleur MA","Blondin G","Messaddeq N","Ollagnier de Choudens S","Eisenmann A","Schmucker S"],"additional_accession":[]},"is_claimable":false,"name":"ISCA1 is essential for mitochondrial Fe<sub>4</sub>S<sub>4</sub> biogenesis in vivo.","description":"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 Fe<sub>4</sub>S<sub>4</sub> proteins. Here we report that mouse ISCA1 and ISCA2 are Fe<sub>2</sub>S<sub>2</sub>-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 Fe<sub>","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 May","modification":"2026-05-04T15:30:55.273Z","creation":"2019-03-27T02:45:24Z"},"accession":"S-EPMC5437272","cross_references":{"pubmed":["28492233"],"doi":["10.1038/ncomms15124"]}}