pubmed-article:8710504 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0017337 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0007009 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0033640 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0017362 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C0162493 | lld:lifeskim |
pubmed-article:8710504 | lifeskim:mentions | umls-concept:C1554184 | lld:lifeskim |
pubmed-article:8710504 | pubmed:issue | 12 | lld:pubmed |
pubmed-article:8710504 | pubmed:dateCreated | 1996-9-9 | lld:pubmed |
pubmed-article:8710504 | pubmed:abstractText | The CSRE (carbon source-responsive element) is a sequence motif responsible for the transcriptional activation of gluconeogenic structural genes in Saccharomyces cerevisiae. We have isolated a regulatory gene, DIL1 (derepression of isocitrate lyase, = CAT8), which is specifically required for derepression of CSRE-dependent genes. Expression of CAT8 is carbon source regulated and requires a functional Cat1p (Snf1p) protein kinase. The derepression defect of CAT8 in a cat1 mutant could be suppressed by a mutant Mig1p repressor protein. Derepression of CAT8 also requires a functional HAP2 gene, suggesting a regulatory connection between respiratory and gluconeogenic genes. Carbon source-dependent protein-CSRE complexes detected in a gel retardation analysis with wild-type extracts were absent in cat8 mutant extracts. However, similar experiments with an epitope-tagged CAT8 gene product in the presence of tag-specific antibodies gave evidence against a direct binding of Cat8p to the CSRE. A constitutively expressed GAL4-CAT8 fusion gene revealed a carbon source-dependent transcriptional activation of a UAS(GAL)-containing reporter gene. Activation mediated by Cat8p was no longer detectable in a cat1 mutant. Thus, biosynthetic control of CAT8 as well as transcriptional activation by Cat8p requires a functional Cat1p protein kinase. A model proposing CAT8 as a specific activator of a transcription factor(s) binding to the CSRE is discussed. | lld:pubmed |
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pubmed-article:8710504 | pubmed:language | eng | lld:pubmed |
pubmed-article:8710504 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8710504 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:8710504 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:8710504 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8710504 | pubmed:month | Jun | lld:pubmed |
pubmed-article:8710504 | pubmed:issn | 0305-1048 | lld:pubmed |
pubmed-article:8710504 | pubmed:author | pubmed-author:SchölerAA | lld:pubmed |
pubmed-article:8710504 | pubmed:author | pubmed-author:SchüllerH JHJ | lld:pubmed |
pubmed-article:8710504 | pubmed:author | pubmed-author:MartensEE | lld:pubmed |
pubmed-article:8710504 | pubmed:author | pubmed-author:RahnerAA | lld:pubmed |
pubmed-article:8710504 | pubmed:author | pubmed-author:GollwitzerBB | lld:pubmed |
pubmed-article:8710504 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8710504 | pubmed:day | 15 | lld:pubmed |
pubmed-article:8710504 | pubmed:volume | 24 | lld:pubmed |
pubmed-article:8710504 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8710504 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8710504 | pubmed:pagination | 2331-7 | lld:pubmed |
pubmed-article:8710504 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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pubmed-article:8710504 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8710504 | pubmed:articleTitle | Dual influence of the yeast Cat1p (Snf1p) protein kinase on carbon source-dependent transcriptional activation of gluconeogenic genes by the regulatory gene CAT8. | lld:pubmed |
pubmed-article:8710504 | pubmed:affiliation | Institut für Mikrobiologie, Biochemie und Genetik, Lehrstuhl Biochemie, Universität Erlangen/Nürnberg, Erlangen, Germany. | lld:pubmed |
pubmed-article:8710504 | pubmed:publicationType | Journal Article | lld:pubmed |