| http://purl.uniprot.org/citations/19349280 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/19349280 | http://www.w3.org/2000/01/rdf-schema#comment | "Perturbation of the cytoplasmic protein folding environment by exposure to oxidative stress-inducing As(III)-containing compounds challenges the ubiquitin-proteasome system. Here we report on mass spectrometric analysis of As(III)-induced changes in the proteasome's composition in samples prepared by stable isotope labeling with amino acids in cell culture, using mammalian cells in which TRP32 (thioredoxin-related protein of 32 kDa; also referred to as TXNL1) was identified as a novel subunit of the 26 S proteasome. Quantitative genetic interaction mapping, using the epistatic miniarray profiling approach, identified a functional connection between TRP32 and the proteasome. Deletion of txl1, the Schizosaccharomyces pombe homolog of TRP32, results in a slow growth phenotype when combined with deletion of cut8, a gene required for normal proteasome localization. Deletion analysis in vivo, chemical cross-linking, and manipulation of the ATP concentration in vitro during proteasome immunopurification revealed that the C-terminal domain of mammalian TRP32 binds the 19 S regulatory particle in proximity to the proteasome substrate binding site. Thiol modification with polyethylene glycol-maleimide showed disulfide bond formation at the active site of TRP32 in cells exposed to As(III). Pulse-chase labeling showed that TRP32 is a stable protein whose half-life of >6 h is surprisingly reduced to 1 h upon exposure of cells to As(III). These findings reveal a previously undescribed thiol reductase at the proteasome's regulatory particle."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m109.002121"xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Krogan N.J."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Wiseman R.L."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Haynes C.M."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Neubert T.A."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Ron D."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Roguev A."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Xu C.F."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Stanhill A."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/author | "Chin K.T."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/pages | "15233-15245"xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/title | "Thioredoxin-related Protein 32 is an arsenite-regulated Thiol Reductase of the proteasome 19 S particle."xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://purl.uniprot.org/core/volume | "284"xsd:string |
| http://purl.uniprot.org/citations/19349280 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19349280 |
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| http://purl.uniprot.org/uniprot/#_B2R960-mappedCitation-19349280 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19349280 |