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Physical and functional interactions of monoubiquitylated transactivators with the proteasome.

Physical and functional interactions of monoubiquitylated transactivators with the proteasome. Research Abstract Details 

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  • Physical and functional interactions of monoubiquitylated transactivators with the proteasome. Abstract Text:

    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.

    Physical and functional interactions of monoubiquitylated transactivators with the proteasome. Publishing Authors By Initials

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    Physical and functional interactions of monoubiquitylated transactivators with the proteasome. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: The Journal of biological chemistry

    VOLUME: 283

    Page Numbers: 21789-98

    Journal Abbreviation: J. Biol. Chem.

    ISSN: 0021-9258

    DAY: 30

    MONTH: 05

    YEAR: 2008

    Physical and functional interactions of monoubiquitylated transactivators with the proteasome. Information

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    LANGUAGE: eng

    NlmUniqueID: 2985121

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    Grant and Affiliation Information for Physical and functional interactions of monoubiquitylated transactivators with the proteasome.

    AFFILIATION: Division of Translational Research and Departments of Internal Medicine and Molecular Biology, University of Texas-Southwestern Medical Center, Dallas, Texas 75390-9185.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: J Biol Chem

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