pubmed-article:8628401 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C0020792 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C0286330 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C1416832 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C1419025 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C1711351 | lld:lifeskim |
pubmed-article:8628401 | lifeskim:mentions | umls-concept:C2003905 | lld:lifeskim |
pubmed-article:8628401 | pubmed:issue | 6566 | lld:pubmed |
pubmed-article:8628401 | pubmed:dateCreated | 1996-6-27 | lld:pubmed |
pubmed-article:8628401 | pubmed:abstractText | The SUG1 gene of Saccharomyces cerevisiae encodes a putative ATPase. Mutations in SUG1 were isolated as suppressors of a mutation in the transcriptional activation domain of GAL4. Sug1 was recently proposed to be a subunit of the RNA polymerase II holoenzyme and to mediate the association of transcriptional activators with holoenzyme. We show here that Sug1 is not a subunit of the holoenzyme, at least in its purified form, but of the 26S proteasome, a large complex of relative molecular-mass 2,000K that catalyses the ATP-dependent degradation of ubiquitin-protein conjugates. Sug1 co-purifies with the proteasome in both conventional and nickel-chelate affinity chromatography. Our observations account for the reduced ubiquitin-dependent proteolysis in sug1 mutants and suggest that the effects of sug1 mutations on transcription are indirect results of defective proteolysis. | lld:pubmed |
pubmed-article:8628401 | pubmed:language | eng | lld:pubmed |
pubmed-article:8628401 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8628401 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8628401 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8628401 | pubmed:month | Feb | lld:pubmed |
pubmed-article:8628401 | pubmed:issn | 0028-0836 | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:YoungR ARA | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:GoldbergA LAL | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:RubinD MDM | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:FinleyDD | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:CourII | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:HengartnerCC | lld:pubmed |
pubmed-article:8628401 | pubmed:author | pubmed-author:WefesII | lld:pubmed |
pubmed-article:8628401 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8628401 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8628401 | pubmed:volume | 379 | lld:pubmed |
pubmed-article:8628401 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8628401 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8628401 | pubmed:pagination | 655-7 | lld:pubmed |
pubmed-article:8628401 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
pubmed-article:8628401 | pubmed:meshHeading | pubmed-meshheading:8628401-... | lld:pubmed |
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pubmed-article:8628401 | pubmed:meshHeading | pubmed-meshheading:8628401-... | lld:pubmed |
pubmed-article:8628401 | pubmed:meshHeading | pubmed-meshheading:8628401-... | lld:pubmed |
pubmed-article:8628401 | pubmed:meshHeading | pubmed-meshheading:8628401-... | lld:pubmed |
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pubmed-article:8628401 | pubmed:meshHeading | pubmed-meshheading:8628401-... | lld:pubmed |
pubmed-article:8628401 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8628401 | pubmed:articleTitle | Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome. | lld:pubmed |
pubmed-article:8628401 | pubmed:affiliation | Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA. | lld:pubmed |
pubmed-article:8628401 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8628401 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8628401 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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