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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
29
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pubmed:dateCreated |
2007-12-6
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pubmed:abstractText |
E153 is a respiratory deficient mutant of Saccharomyces cerevisiae with a mutation in the active site of the Sit4p protein phosphatase. Measurements of mitochondrial respiration and cytochromes indicate that the mutation suppresses glucose repression. The escape from catabolite repression is accompanied by a marked reduction of the transcriptional repressor Mig1p. The presence of normal levels of MIG1 mRNA in the mutant and its association with the polysome fraction suggests that depletion of Mig1p is the result of protein degradation. This study shows that in addition to phosphorylation by Snf1p, the transcriptional repressor activity of Mig1p is also regulated by a post-transcriptional Sit4p-dependent pathway. Our evidence suggests that this pathway involves turnover of Mig1p.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-11782424,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-12930741,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-1310793,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-1316273,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-133820,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-14718557,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-1656218,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-16764994,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-170284,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2038333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2115121,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2167835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2215420,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2445751,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2537149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2692852,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-2826015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-3333305,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-414220,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-6310321,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-6310324,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-6366513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-6392017,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-7724528,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-8056322,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-8208248,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-9285828,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-9286668,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-9618445,
http://linkedlifedata.com/resource/pubmed/commentcorrection/18022394-9774644
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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/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ISF1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MIG1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 2,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Repressor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SIT4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SNF1-related protein kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0014-5793
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
11
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pubmed:volume |
581
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5658-63
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:18022394-Alleles,
pubmed-meshheading:18022394-DNA-Binding Proteins,
pubmed-meshheading:18022394-Gene Expression Regulation, Fungal,
pubmed-meshheading:18022394-Models, Biological,
pubmed-meshheading:18022394-Mutation,
pubmed-meshheading:18022394-Phenotype,
pubmed-meshheading:18022394-Phosphorylation,
pubmed-meshheading:18022394-Protein Phosphatase 2,
pubmed-meshheading:18022394-Protein-Serine-Threonine Kinases,
pubmed-meshheading:18022394-Repressor Proteins,
pubmed-meshheading:18022394-Saccharomyces cerevisiae,
pubmed-meshheading:18022394-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:18022394-Signal Transduction
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pubmed:year |
2007
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pubmed:articleTitle |
SIT4 regulation of Mig1p-mediated catabolite repression in Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Biological Sciences, Columbia University, New York, NY 10027, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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