Abstract
THE SUG1 gene of Saccharomyces cerevisiae encodes a putative ATPase. Mutations in SUG1 were isolated1 as suppressors of a mutation in the transcriptional activation domain of GAL4. Sugl was recently proposed to be a subunit of the RNA polymerase II holoenzyme and to mediate the association of transcriptional activators with holoenzyme2. We show here that Sugl is not a subunit of the holoenzyme, at least in its purified form, but of the 26S proteasome3,4, a large complex of relative molecular-mass 2,OOOK that catalyses the ATP-dependent degradation of ubiqui-tin–protein conjugates. Sugl co-purifies with the proteasome in both conventional and nickel-chelate affinity chromatography. Our observations account for the reduced ubiquitin-dependent proteolysis in sug1 mutants5 and suggest that the effects of sug1 mutations on transcription are indirect results of defective proteolysis.
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Rubin, D., Coux, O., Wefes, I. et al. Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. Nature 379, 655–657 (1996). https://doi.org/10.1038/379655a0
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DOI: https://doi.org/10.1038/379655a0
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