{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Maio N"],"funding":["Intramural NIH HHS"],"pagination":["945-953.e6"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12285277"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["25(4)"],"pubmed_abstract":["The iron-sulfur (Fe-S) cluster of the Rieske protein, UQCRFS1, is essential for Complex III (CIII) activity, though the mechanism for Fe-S cluster transfer has not previously been elucidated. Recent studies have shown that the co-chaperone HSC20, essential for Fe-S cluster biogenesis of SDHB, directly binds LYRM7, formerly described as a chaperone that stabilizes UQCRFS1 prior to its insertion into CIII. Here we report that a transient subcomplex involved in CIII assembly, composed of LYRM7 bound to UQCRFS1, interacts with components of an Fe-S transfer complex, consisting of HSC20, its cognate chaperone HSPA9, and the holo-scaffold ISCU. Binding of HSC20 to the LYR motif of LYRM7 in a pre-assembled UQCRFS1-LYRM7 intermediate in the mitochondrial matrix facilitates Fe-S cluster transfer to"],"journal":["Cell metabolism"],"pubmed_title":["A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III."],"pmcid":["PMC12285277"],"funding_grant_id":["Z01 HD008814"],"pubmed_authors":["Maio N","Singh A","Kim KS","Rouault TA"],"additional_accession":[]},"is_claimable":false,"name":"A Single Adaptable Cochaperone-Scaffold Complex Delivers Nascent Iron-Sulfur Clusters to Mammalian Respiratory Chain Complexes I-III.","description":"The iron-sulfur (Fe-S) cluster of the Rieske protein, UQCRFS1, is essential for Complex III (CIII) activity, though the mechanism for Fe-S cluster transfer has not previously been elucidated. Recent studies have shown that the co-chaperone HSC20, essential for Fe-S cluster biogenesis of SDHB, directly binds LYRM7, formerly described as a chaperone that stabilizes UQCRFS1 prior to its insertion into CIII. Here we report that a transient subcomplex involved in CIII assembly, composed of LYRM7 bound to UQCRFS1, interacts with components of an Fe-S transfer complex, consisting of HSC20, its cognate chaperone HSPA9, and the holo-scaffold ISCU. Binding of HSC20 to the LYR motif of LYRM7 in a pre-assembled UQCRFS1-LYRM7 intermediate in the mitochondrial matrix facilitates Fe-S cluster transfer to","dates":{"release":"2017-01-01T00:00:00Z","publication":"2017 Apr","modification":"2026-03-17T13:43:17.892Z","creation":"2025-08-16T03:05:42.543Z"},"accession":"S-EPMC12285277","cross_references":{"pubmed":["28380382"],"doi":["10.1016/j.cmet.2017.03.010"]}}