TY - JOUR
T1 - Physical and functional interactions of monoubiquitylated transactivators with the proteasome
AU - Archer, Chase T.
AU - Burdine, Lyle
AU - Liu, Bo
AU - Ferdous, Anwarul
AU - Johnston, Stephen Albert
AU - Kodadek, Thomas
PY - 2008/8/1
Y1 - 2008/8/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=52049114924&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=52049114924&partnerID=8YFLogxK
U2 - 10.1074/jbc.M803075200
DO - 10.1074/jbc.M803075200
M3 - Article
C2 - 18515799
AN - SCOPUS:52049114924
SN - 0021-9258
VL - 283
SP - 21789
EP - 21798
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 31
ER -