| http://purl.uniprot.org/citations/29309586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29309586 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/29309586 | http://www.w3.org/2000/01/rdf-schema#comment | "Iron-sulfur (Fe-S) clusters are cofactors in hundreds of proteins involved in multiple cellular processes, including mitochondrial respiration, the maintenance of genome stability, ribosome biogenesis and translation. Fe-S cluster biogenesis is performed by multiple enzymes that are highly conserved throughout evolution, and mutations in numerous biogenesis factors are now recognized to cause a wide range of previously uncategorized rare human diseases. Recently, a complex formed of components of the cytoplasmic Fe-S cluster assembly (CIA) machinery, consisting of CIAO1, FAM96B and MMS19, was found to deliver Fe-S clusters to a subset of proteins involved in DNA metabolism, but it was unclear how this complex acquired its fully synthesized Fe-S clusters, because Fe-S clusters have been alleged to be assembled de novo solely in the mitochondrial matrix. Here, we investigated the potential role of the human cochaperone HSC20 in cytosolic Fe-S assembly and found that HSC20 assists Fe-S cluster delivery to cytosolic and nuclear Fe-S proteins. Cytosolic HSC20 (C-HSC20) mediated complex formation between components of the cytosolic Fe-S biogenesis pathway (ISC), including the primary scaffold, ISCU1, and the cysteine desulfurase, NFS1, and the CIA targeting complex, consisting of CIAO1, FAM96B and MMS19, to facilitate Fe-S cluster insertion into cytoplasmic and nuclear Fe-S recipients. Thus, C-HSC20 integrates initial Fe-S biosynthesis with the transfer activities of the CIA targeting system. Our studies demonstrate that a novel cytosolic pathway functions in parallel to the mitochondrial ISC to perform de novo Fe-S biogenesis, and to escort Fe-S clusters to cytoplasmic and nuclear proteins."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddy004"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.org/dc/terms/identifier | "doi:10.1093/hmg/ddy004"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Singh A."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Singh A."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Kim K.S."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Kim K.S."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Maio N."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Maio N."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Rouault T.A."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/author | "Rouault T.A."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/date | "2018"xsd:gYear |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/name | "Hum. Mol. Genet."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/pages | "837-852"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/pages | "837-852"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/title | "Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the CIAO1-mediated transfer to recipients."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/title | "Cytosolic HSC20 integrates de novo iron-sulfur cluster biogenesis with the CIAO1-mediated transfer to recipients."xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/volume | "27"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://purl.uniprot.org/core/volume | "27"xsd:string |
| http://purl.uniprot.org/citations/29309586 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29309586 |
| http://purl.uniprot.org/citations/29309586 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/29309586 |