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Article: Thioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle

TitleThioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle
Authors
Issue Date2009
Citation
Journal of Biological Chemistry, 2009, v. 284, n. 22, p. 15233-15245 How to Cite?
AbstractPerturbation 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 crosslinking, 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. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.
Persistent Identifierhttp://hdl.handle.net/10722/205708
ISSN
2015 Impact Factor: 4.258
2015 SCImago Journal Rankings: 3.151
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorWiseman, R. Luke-
dc.contributor.authorChin, Kingtung-
dc.contributor.authorHaynes, Cole M.-
dc.contributor.authorStanhill, Ariel-
dc.contributor.authorXu, Chongfeng-
dc.contributor.authorRoguev, Assen-
dc.contributor.authorKrogan, Nevan J.-
dc.contributor.authorNeubert, Thomas A.-
dc.contributor.authorRon, David-
dc.date.accessioned2014-10-06T08:02:14Z-
dc.date.available2014-10-06T08:02:14Z-
dc.date.issued2009-
dc.identifier.citationJournal of Biological Chemistry, 2009, v. 284, n. 22, p. 15233-15245-
dc.identifier.issn0021-9258-
dc.identifier.urihttp://hdl.handle.net/10722/205708-
dc.description.abstractPerturbation 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 crosslinking, 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. © 2009 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.languageeng-
dc.relation.ispartofJournal of Biological Chemistry-
dc.titleThioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle-
dc.typeArticle-
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1074/jbc.M109.002121-
dc.identifier.pmid19349280-
dc.identifier.scopuseid_2-s2.0-67649363856-
dc.identifier.volume284-
dc.identifier.issue22-
dc.identifier.spage15233-
dc.identifier.epage15245-
dc.identifier.eissn1083-351X-
dc.identifier.isiWOS:000266288200058-

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