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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
4957
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pubmed:dateCreated |
1990-6-26
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pubmed:abstractText |
In Saccharomyces cerevisiae, the product of the CDC25 gene controls the RAS-mediated production of adenosine 3',5'-monophosphate (cAMP). In vivo the carboxyl-terminal third of the CDC25 gene product is sufficient for the activation of adenylate cyclase. The 3'-terminal part of SCD25, a gene of S. cerevisiae structurally related to CDC25, can suppress the requirement for CDC25. Partially purified preparations of the carboxy-terminal domain of the SCD25 gene product enhanced the exchange rate of guanosine diphosphate (GDP) to guanosine triphosphate (GTP) of pure RAS2 protein by stimulating the release of GDP. This protein fragment had a similar effect on the human c-H-ras-encoded p21 protein. Thus, the SCD25 carboxyl-terminal domain can enhance the regeneration of the active form of RAS proteins.
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pubmed:commentsCorrections |
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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/CDC25 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine Nucleotides,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Diphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/Guanosine Triphosphate,
http://linkedlifedata.com/resource/pubmed/chemical/HRAS protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins p21(ras),
http://linkedlifedata.com/resource/pubmed/chemical/RAS2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ras-GRF1
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0036-8075
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
248
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
866-8
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pubmed:dateRevised |
2009-12-11
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pubmed:meshHeading |
pubmed-meshheading:2188363-Cell Cycle Proteins,
pubmed-meshheading:2188363-Escherichia coli,
pubmed-meshheading:2188363-Fungal Proteins,
pubmed-meshheading:2188363-Genes, Fungal,
pubmed-meshheading:2188363-Guanine Nucleotides,
pubmed-meshheading:2188363-Guanosine Diphosphate,
pubmed-meshheading:2188363-Guanosine Triphosphate,
pubmed-meshheading:2188363-Humans,
pubmed-meshheading:2188363-Kinetics,
pubmed-meshheading:2188363-Peptide Fragments,
pubmed-meshheading:2188363-Plasmids,
pubmed-meshheading:2188363-Proto-Oncogene Proteins,
pubmed-meshheading:2188363-Proto-Oncogene Proteins p21(ras),
pubmed-meshheading:2188363-Recombinant Fusion Proteins,
pubmed-meshheading:2188363-Saccharomyces cerevisiae,
pubmed-meshheading:2188363-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:2188363-Transfection,
pubmed-meshheading:2188363-ras Proteins,
pubmed-meshheading:2188363-ras-GRF1
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pubmed:year |
1990
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pubmed:articleTitle |
Enhancement of the GDP-GTP exchange of RAS proteins by the carboxyl-terminal domain of SCD25.
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pubmed:affiliation |
Laboratoire de Biochimie, URA 240 du CNRS, Ecole Polytechnique, Palaiseau, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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