| Physical and functional interactions of monoubiquitylated transactivators with the proteasome. | |
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MedLine Citation:
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PMID: 18515799 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Destabilization of activator-DNA complexes by the proteasomal ATPases can inhibit transcription by limiting activator interaction with DNA. Modification of the activator by monoubiquitylation protects the activator from this destabilization activity. In this study, we probe the mechanism of this protective effect of monoubiquitylation. Using novel label transfer and chemical cross-linking techniques, we show that ubiquitin contacts the ATPase complex directly, apparently via Rpn1 and Rpt1. This interaction results in the dissociation of the activation domain-ATPase complex via an allosteric process. A model is proposed in which activator monoubiquitylation serves to limit the lifetime of the activator-ATPase complex interaction and thus the ability of the ATPases to unfold the activator and dissociate the protein-DNA complex. |
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Authors:
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Chase T Archer; Lyle Burdine; Bo Liu; Anwarul Ferdous; Stephen Albert Johnston; Thomas Kodadek |
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Publication Detail:
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Type: Journal Article; Research Support, N.I.H., Extramural Date: 2008-05-30 |
Journal Detail:
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Title: The Journal of biological chemistry Volume: 283 ISSN: 0021-9258 ISO Abbreviation: J. Biol. Chem. Publication Date: 2008 Aug |
Date Detail:
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Created Date: 2008-07-28 Completed Date: 2008-09-22 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 2985121R Medline TA: J Biol Chem Country: United States |
Other Details:
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Languages: eng Pagination: 21789-98 Citation Subset: IM |
Affiliation:
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Division of Translational Research and Department of Internal Medicine, University of Texas-Southwestern Medical Center, Dallas, TX 75390-9185, USA. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Adenosine Triphosphatases
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chemistry,
metabolism Cross-Linking Reagents / pharmacology DNA / chemistry DNA-Binding Proteins / metabolism Hela Cells Humans Hydrolysis Inhibitory Concentration 50 Models, Chemical Proteasome Endopeptidase Complex / chemistry Protein Binding Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / metabolism Transcriptional Activation* Ubiquitin / chemistry* |
| Grant Support | |
ID/Acronym/Agency:
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GM 71833/GM/NIGMS NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Cross-Linking Reagents; 0/DNA-Binding Proteins; 0/RPN1 protein, S cerevisiae; 0/Saccharomyces cerevisiae Proteins; 0/Ubiquitin; 9007-49-2/DNA; EC 3.4.25.1/Proteasome Endopeptidase Complex; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.3/RPT1 protein, S cerevisiae |
| Comments/Corrections | |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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