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- Publisher Website: 10.1074/jbc.M109.002121
- Scopus: eid_2-s2.0-67649363856
- PMID: 19349280
- WOS: WOS:000266288200058
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Article: Thioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle
Title | Thioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle |
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Authors | |
Issue Date | 2009 |
Citation | Journal of Biological Chemistry, 2009, v. 284, n. 22, p. 15233-15245 How to Cite? |
Abstract | 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 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 Identifier | http://hdl.handle.net/10722/205708 |
ISSN | 2020 Impact Factor: 5.157 2023 SCImago Journal Rankings: 1.766 |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | Wiseman, R. Luke | - |
dc.contributor.author | Chin, Kingtung | - |
dc.contributor.author | Haynes, Cole M. | - |
dc.contributor.author | Stanhill, Ariel | - |
dc.contributor.author | Xu, Chongfeng | - |
dc.contributor.author | Roguev, Assen | - |
dc.contributor.author | Krogan, Nevan J. | - |
dc.contributor.author | Neubert, Thomas A. | - |
dc.contributor.author | Ron, David | - |
dc.date.accessioned | 2014-10-06T08:02:14Z | - |
dc.date.available | 2014-10-06T08:02:14Z | - |
dc.date.issued | 2009 | - |
dc.identifier.citation | Journal of Biological Chemistry, 2009, v. 284, n. 22, p. 15233-15245 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10722/205708 | - |
dc.description.abstract | 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 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.language | eng | - |
dc.relation.ispartof | Journal of Biological Chemistry | - |
dc.title | Thioredoxin-related protein 32 is an arsenite-regulated thiol reductase of the proteasome 19 S particle | - |
dc.type | Article | - |
dc.description.nature | link_to_subscribed_fulltext | - |
dc.identifier.doi | 10.1074/jbc.M109.002121 | - |
dc.identifier.pmid | 19349280 | - |
dc.identifier.scopus | eid_2-s2.0-67649363856 | - |
dc.identifier.volume | 284 | - |
dc.identifier.issue | 22 | - |
dc.identifier.spage | 15233 | - |
dc.identifier.epage | 15245 | - |
dc.identifier.eissn | 1083-351X | - |
dc.identifier.isi | WOS:000266288200058 | - |
dc.identifier.issnl | 0021-9258 | - |