| http://purl.uniprot.org/citations/27519415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27519415 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/27519415 | http://www.w3.org/2000/01/rdf-schema#comment | "Cells contain hundreds of proteins that require iron cofactors for activity. Iron cofactors are synthesized in the cell, but the pathways involved in distributing heme, iron-sulfur clusters, and ferrous/ferric ions to apoproteins remain incompletely defined. In particular, cytosolic monothiol glutaredoxins and BolA-like proteins have been identified as [2Fe-2S]-coordinating complexes in vitro and iron-regulatory proteins in fungi, but it is not clear how these proteins function in mammalian systems or how this complex might affect Fe-S proteins or the cytosolic Fe-S assembly machinery. To explore these questions, we use quantitative immunoprecipitation and live cell proximity-dependent biotinylation to monitor interactions between Glrx3, BolA2, and components of the cytosolic iron-sulfur cluster assembly system. We characterize cytosolic Glrx3·BolA2 as a [2Fe-2S] chaperone complex in human cells. Unlike complexes formed by fungal orthologs, human Glrx3-BolA2 interaction required the coordination of Fe-S clusters, whereas Glrx3 homodimer formation did not. Cellular Glrx3·BolA2 complexes increased 6-8-fold in response to increasing iron, forming a rapidly expandable pool of Fe-S clusters. Fe-S coordination by Glrx3·BolA2 did not depend on Ciapin1 or Ciao1, proteins that bind Glrx3 and are involved in cytosolic Fe-S cluster assembly and distribution. Instead, Glrx3 and BolA2 bound and facilitated Fe-S incorporation into Ciapin1, a [2Fe-2S] protein functioning early in the cytosolic Fe-S assembly pathway. Thus, Glrx3·BolA is a [2Fe-2S] chaperone complex capable of transferring [2Fe-2S] clusters to apoproteins in human cells."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m116.744946"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m116.744946"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Philpott C.C."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Philpott C.C."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Frey A.G."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Frey A.G."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Palenchar D.J."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Palenchar D.J."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Wildemann J.D."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/author | "Wildemann J.D."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/date | "2016"xsd:gYear |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/pages | "22344-22356"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/pages | "22344-22356"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/title | "A glutaredoxin-BolA complex serves as an iron-sulfur cluster chaperone for the cytosolic cluster assembly machinery."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/title | "A glutaredoxin-BolA complex serves as an iron-sulfur cluster chaperone for the cytosolic cluster assembly machinery."xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/volume | "291"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://purl.uniprot.org/core/volume | "291"xsd:string |
| http://purl.uniprot.org/citations/27519415 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27519415 |
| http://purl.uniprot.org/citations/27519415 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/27519415 |