Physical and functional interactions of monoubiquitylated transactivators with the proteasome

被引：33

作者：

Archer, Chase T. ^{[1
]}

Burdine, Lyle ^{[1
]}

Liu, Bo ^{[1
]}

Ferdous, Anwarul ^{[2
]}

Johnston, Stephen Albert ^{[2
]}

Kodadek, Thomas ^{[1
,2
,3
]}

机构：

[1] Univ Texas SW Med Ctr Dallas, Div Translat Res, Dallas, TX 75390 USA

[2] Univ Texas SW Med Ctr Dallas, Dept Internal Med, Dallas, TX 75390 USA

[3] Univ Texas SW Med Ctr Dallas, Dept Mol Biol, Dallas, TX 75390 USA

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2008年 / 283卷 / 31期

关键词：

D O I：

10.1074/jbc.M803075200

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Destabilization of activator-DNA complexes by the proteasomal ATPases can inhibit transcription by limiting activator interaction with DNA. Modification of the activator by monou-biquitylation 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.

引用

页码：21789 / 21798

页数：10

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