Journal
CELL
Volume 120, Issue 6, Pages 887-899Publisher
CELL PRESS
DOI: 10.1016/j.cell.2004.12.025
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Funding
- NCI NIH HHS [CA13106] Funding Source: Medline
- NIAID NIH HHS [AI044009] Funding Source: Medline
- NIGMS NIH HHS [GM067728] Funding Source: Medline
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We report here that the prototypical yeast transcription factor Gal4 undergoes two distinct modes of ubiquitin-mediated proteolysis: one that occurs independent of transcription and restricts Gal4 function, and another that is transcription coupled and essential for productive activation of Gal4 target genes. Destruction of transcriptionally active Gal4 depends on an F box protein called Dsgl/Mdm30. In the absence of Dsg1, Gal4 is stable, nonubiquitylated, and unable to productively stimulate transcription. Analysis of the phenotype of dsgl-nuil yeast reveals a striking disconnect between GAL gene RNA and protein levels; in the absence of Dsgl, Gal4 target genes are transcribed, but the resulting RNAs are not translated. The translational defects of these RNAs are related to defects in phosphorylation of the RNA polymerase 11 carboxy-terminal domain, which in turn affects recruitment of RNA processing machinery. We propose that Gal4 ubiquitylation and destruction are required for initiation-competent transcription complexes to transition to fully mature elongating complexes capable of appropriate mRNA processing.
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