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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
1994-7-6
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pubmed:abstractText |
The GCN2 (general control kinase 2) protein is an eIF2-alpha (eukaryotic initiation factor alpha) kinase which mediates translational derepression of the yeast general control transcriptional activator, GCN4, upon amino-acid starvation. We isolated and characterized GCN2 mutations differentially affecting GCN2 function. Mutations mapping in, or close to, the ATP-binding site of the kinase moiety result in constitutively activated GCN2 molecules. A C-terminal regulatory mutation dramatically affects translation initiation rates resulting in pleiotropic phenotypes. The effect of mutations in both regions were found to depend on eIF2-alpha phosphorylation. We have demonstrated that GCN2 mutants have altered autophosphorylation activities in vitro, depending on the presence or absence of a wild-type GCN2 gene and that GCN2 elutes in gel-filtration chromatography fractions with high apparent molecular mass. Both these genetic and biochemical findings suggest that GCN2 functioning might involve polymerization to form dimers or tetramers.
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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/Amino Acids,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/GCN2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
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 |
May
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pubmed:issn |
0378-1119
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
27
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pubmed:volume |
143
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pubmed:geneSymbol |
GCN2,
GCN4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
21-7
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8200534-Amino Acids,
pubmed-meshheading:8200534-Chromatography, Gel,
pubmed-meshheading:8200534-DNA Mutational Analysis,
pubmed-meshheading:8200534-DNA-Binding Proteins,
pubmed-meshheading:8200534-Eukaryotic Initiation Factor-2,
pubmed-meshheading:8200534-Fungal Proteins,
pubmed-meshheading:8200534-Gene Expression Regulation, Enzymologic,
pubmed-meshheading:8200534-Gene Expression Regulation, Fungal,
pubmed-meshheading:8200534-Genes, Fungal,
pubmed-meshheading:8200534-Mutation,
pubmed-meshheading:8200534-Peptide Initiation Factors,
pubmed-meshheading:8200534-Peptide Mapping,
pubmed-meshheading:8200534-Phosphorylation,
pubmed-meshheading:8200534-Protein Biosynthesis,
pubmed-meshheading:8200534-Protein Kinases,
pubmed-meshheading:8200534-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8200534-RNA, Messenger,
pubmed-meshheading:8200534-Repressor Proteins,
pubmed-meshheading:8200534-Ribosomes,
pubmed-meshheading:8200534-Saccharomyces cerevisiae,
pubmed-meshheading:8200534-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8200534-Signal Transduction,
pubmed-meshheading:8200534-Transcription Factors
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pubmed:year |
1994
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pubmed:articleTitle |
Genetic and biochemical evidence for yeast GCN2 protein kinase polymerization.
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pubmed:affiliation |
Institute of Molecular Biology and Biotechnology, Foundation for Research and Technology, Heraklion, Crete, Greece.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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