| http://purl.uniprot.org/citations/21299470 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/21299470 | http://www.w3.org/2000/01/rdf-schema#comment | "Monothiol glutaredoxins (Grxs) with a noncanonical CGFS active site are found in all kingdoms of life. They include members with a single domain and thioredoxin-Grx fusion proteins. In Saccharomyces cerevisiae, the multidomain Grx3 and Grx4 play an essential role in intracellular iron trafficking. This crucial task is mediated by an essential Fe/S cofactor. This study shows that this unique physiological role cannot be executed by single domain Grxs, because the thioredoxin domain is indispensable for function in vivo. Mutational analysis revealed that a CPxS active site motif is fully compatible with Fe/S cluster binding on Grx4, while a dithiol active site results in cofactor destabilization and a moderate impairment of in vivo function. These requirements for Fe/S cofactor stabilization on Grx4 are virtually the opposite of those previously reported for single domain Grxs. Grx4 functions as iron sensor for the iron-sensing transcription factor Aft1 in S. cerevisiae. We found that Aft1 binds to a conserved binding site at the C-terminus of Grx4. This interaction is essential for the regulation of Aft1. Collectively, our analysis demonstrates that the multidomain monothiol Grxs form a unique protein family distinct from that of the single domain Grxs."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.org/dc/terms/identifier | "doi:10.1089/ars.2010.3811"xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Hoffmann B."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Lill R."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Berndt C."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Lillig C.H."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Muhlenhoff U."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Uzarska M.A."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Godoy J.R."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/author | "Haunhorst P."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/date | "2011"xsd:gYear |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/name | "Antioxid Redox Signal"xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/pages | "19-30"xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/title | "The multidomain thioredoxin-monothiol glutaredoxins represent a distinct functional group."xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://purl.uniprot.org/core/volume | "15"xsd:string |
| http://purl.uniprot.org/citations/21299470 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/21299470 |
| http://purl.uniprot.org/citations/21299470 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/21299470 |
| http://purl.uniprot.org/uniprot/#_P22149-mappedCitation-21299470 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21299470 |
| http://purl.uniprot.org/uniprot/#_P32642-mappedCitation-21299470 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/21299470 |
| http://purl.uniprot.org/uniprot/P22149 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21299470 |
| http://purl.uniprot.org/uniprot/P32642 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/21299470 |