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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
11
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pubmed:dateCreated |
1991-7-19
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pubmed:abstractText |
The substrates of ubiquitin-dependent proteolytic pathways include both damaged or otherwise abnormal proteins and undamaged proteins that are naturally short-lived. Few specific examples of the latter class have been identified, however. Previous work has shown that the cell type-specific MAT alpha 2 repressor of the yeast Saccharomyces cerevisiae is an extremely short-lived protein. We now demonstrate that alpha 2 is conjugated to ubiquitin in vivo. More than one lysine residue of alpha 2 can be joined to ubiquitin, and some of the ubiquitin moieties form a Lys48-linked multiubiquitin chain. Overexpression of degradation-impaired ubiquitin variants was used to show that at least a significant fraction of alpha 2 degradation is dependent on its ubiquitination.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-1846030,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2111732,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2154373,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2167175,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2193438,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2276626,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2455217,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2513489,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2538468,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2538923,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2566918,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2659436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-2696178,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3018930,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3029116,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3038523,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3043180,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3073106,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3323813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-3915782,
http://linkedlifedata.com/resource/pubmed/commentcorrection/1647011-6327060
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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 |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
88
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4606-10
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:1647011-Amino Acid Sequence,
pubmed-meshheading:1647011-Fungal Proteins,
pubmed-meshheading:1647011-Genes, Fungal,
pubmed-meshheading:1647011-Genes, myc,
pubmed-meshheading:1647011-Homeodomain Proteins,
pubmed-meshheading:1647011-Kinetics,
pubmed-meshheading:1647011-Molecular Sequence Data,
pubmed-meshheading:1647011-Mutagenesis, Site-Directed,
pubmed-meshheading:1647011-Plasmids,
pubmed-meshheading:1647011-Protein Processing, Post-Translational,
pubmed-meshheading:1647011-Repressor Proteins,
pubmed-meshheading:1647011-Saccharomyces cerevisiae,
pubmed-meshheading:1647011-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:1647011-Transcription, Genetic,
pubmed-meshheading:1647011-Ubiquitins
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pubmed:year |
1991
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pubmed:articleTitle |
The short-lived MAT alpha 2 transcriptional regulator is ubiquitinated in vivo.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Chicago, IL 60637.
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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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