Regulation of transcriptional activation domain function by ubiquitin.

Salghetti SE, Caudy AA, Chenoweth JG, Tansey WP
Science. 2001 293 (5535): 1651-3

PMID: 11463878 · DOI:10.1126/science.1062079

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.

MeSH Terms (20)

Bacterial Proteins Cysteine Endopeptidases DNA Replication F-Box Proteins Genes, Reporter Herpes Simplex Virus Protein Vmw65 Ligases Multienzyme Complexes Promoter Regions, Genetic Proteasome Endopeptidase Complex Protein Structure, Tertiary Recombinant Fusion Proteins Repressor Proteins Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins Serine Endopeptidases Transcriptional Activation Ubiquitin-Protein Ligase Complexes Ubiquitin-Protein Ligases Ubiquitins

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