Regulation of transcriptional activation domain function by ubiquitin

Salghetti, S. E., Caudy, A. A., Chenoweth, J. G., Tansey, W. P. (August 2001) Regulation of transcriptional activation domain function by ubiquitin. Science, 293 (5535). pp. 1651-1653. ISSN 0036-8075

URL: http://www.ncbi.nlm.nih.gov/pubmed/11463878
DOI: 10.1126/science.1062079

Abstract

The ability of transcriptional activation domains (TADs) to signal ubiquitin-mediated proteolysis suggests an involvement of the ubiquitin-proteasome pathway in transcription. To probe this involvement, we asked how ubiquitylation regulates the activity of a transcription factor containing the VP16 TAD. We show that the VP16 TAD signals ubiquitylation through the Met30 ubiquitin-ligase and that Met30 is also required for the VP16 TAD to activate transcription. The requirement for Met30 in transcription is circumvented by fusion of ubiquitin to the VP16 activator, demonstrating that activator ubiquitylation is essential for transcriptional activation. We propose that ubiquitylation regulates TAD function by serving as a dual signal for activation and activator destruction.

Item Type: Paper
Uncontrolled Keywords: MEDIATED PROTEOLYSIS DNA-REPLICATION DEGRADATION PROTEASOME PROTEINS COMPLEX SIGNAL CHAIN MET4
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > transcription
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein ubiquitination
CSHL Authors:
Communities: CSHL labs > Tansey lab
Watson School > Publications
Depositing User: Matt Covey
Date: August 2001
Date Deposited: 17 Jan 2014 15:16
Last Modified: 19 Sep 2014 13:53
Related URLs:
URI: http://repository.cshl.edu/id/eprint/29294

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