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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6566
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pubmed:dateCreated |
1996-6-27
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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.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ATP dependent 26S protease,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GAL4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Hydrolases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteasome Endopeptidase Complex,
http://linkedlifedata.com/resource/pubmed/chemical/RPT6 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0028-0836
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
379
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
655-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8628401-Adenosine Triphosphatases,
pubmed-meshheading:8628401-Amino Acid Sequence,
pubmed-meshheading:8628401-DNA-Binding Proteins,
pubmed-meshheading:8628401-Fungal Proteins,
pubmed-meshheading:8628401-Molecular Sequence Data,
pubmed-meshheading:8628401-Peptide Hydrolases,
pubmed-meshheading:8628401-Proteasome Endopeptidase Complex,
pubmed-meshheading:8628401-Repressor Proteins,
pubmed-meshheading:8628401-Saccharomyces cerevisiae,
pubmed-meshheading:8628401-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8628401-Transcription Factors
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pubmed:year |
1996
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pubmed:articleTitle |
Identification of the gal4 suppressor Sug1 as a subunit of the yeast 26S proteasome.
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pubmed:affiliation |
Department of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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