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http://purl.uniprot.org/citations/23615440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23615440http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/23615440http://www.w3.org/2000/01/rdf-schema#comment"The mitochondrial Hsp70 chaperone Ssq1 plays a dedicated role in the maturation of iron-sulfur (Fe/S) proteins, an essential process of mitochondria. Similar to its bacterial orthologue HscA, Ssq1 binds to the scaffold protein Isu1, thereby facilitating dissociation of the newly synthesized Fe/S cluster on Isu1 and its transfer to target apoproteins. Here we use in vivo and in vitro approaches to show that Ssq1 also interacts with the monothiol glutaredoxin 5 (Grx5) at a binding site different from that of Isu1. Grx5 binding does not stimulate the ATPase activity of Ssq1 and is most pronounced for the ADP-bound form of Ssq1, which interacts with Isu1 most tightly. The vicinity of Isu1 and Grx5 on the Hsp70 chaperone facilitates rapid Fe/S cluster transfer from Isu1 to Grx5. Grx5 and its bound Fe/S cluster are required for maturation of all cellular Fe/S proteins, regardless of the type of bound Fe/S cofactor and subcellular localization. Hence Grx5 functions as a late-acting component of the core Fe/S cluster (ISC) assembly machinery linking the Fe/S cluster synthesis reaction on Isu1 with late assembly steps involving Fe/S cluster targeting to dedicated apoproteins."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e12-09-0644"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.org/dc/terms/identifier"doi:10.1091/mbc.e12-09-0644"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Lill R."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Lill R."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Freibert S.A."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Freibert S.A."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Muehlenhoff U."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Muehlenhoff U."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Uzarska M.A."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Uzarska M.A."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Dutkiewicz R."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/author"Dutkiewicz R."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/date"2013"xsd:gYear
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/name"Mol. Biol. Cell"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/pages"1830-1841"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/pages"1830-1841"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/title"The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/title"The mitochondrial Hsp70 chaperone Ssq1 facilitates Fe/S cluster transfer from Isu1 to Grx5 by complex formation."xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/volume"24"xsd:string
http://purl.uniprot.org/citations/23615440http://purl.uniprot.org/core/volume"24"xsd:string