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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
12
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pubmed:dateCreated |
1992-12-29
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pubmed:abstractText |
GCN2 is a protein kinase in Saccharomyces cerevisiae that is required for increased expression of the transcriptional activator GCN4 in amino acid-starved cells. GCN2 stimulates GCN4 synthesis at the translational level by phosphorylating the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2). We identified a truncated form of the GLC7 gene, encoding the catalytic subunit of a type 1 protein phosphatase, by its ability to restore derepression of GCN4 expression in a strain containing the partially defective gcn2-507 allele. Genetic analysis suggests that the truncated GLC7 allele has a dominant negative phenotype, reducing the level of native type 1 protein phosphatase activity in the cell. The truncated form of GLC7 does not suppress the regulatory defect associated with a gcn2 deletion or a mutation in the phosphorylation site of eIF-2 alpha (Ser-51). In addition, the presence of multiple copies of wild-type GLC7 impairs the derepression of GCN4 that occurs in response to amino acid starvation or dominant-activating mutations in GCN2. These findings suggest that the phosphatase activity of GLC7 acts in opposition to the kinase activity of GCN2 in modulating the level of eIF-2 alpha phosphorylation and the translational efficiency of GCN4 mRNA. This conclusion is supported by biochemical studies showing that the truncated GLC7 allele increases the level of eIF-2 alpha phosphorylation in the gcn2-507 mutant to a level approaching that seen in wild-type cells under starvation conditions. The truncated GLC7 allele also leads to reduced glycogen accumulation, indicating that this protein phosphatase is involved in regulating diverse metabolic pathways in yeast cells.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/1333044-1310938,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/1333044-786628
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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 |
Dec
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pubmed:issn |
0270-7306
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
12
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pubmed:geneSymbol |
GCN4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5700-10
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pubmed:dateRevised |
2010-9-7
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pubmed:meshHeading |
pubmed-meshheading:1333044-Histidine,
pubmed-meshheading:1333044-Phosphoprotein Phosphatases,
pubmed-meshheading:1333044-Phosphorylation,
pubmed-meshheading:1333044-Saccharomyces cerevisiae,
pubmed-meshheading:1333044-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:1333044-Protein Biosynthesis,
pubmed-meshheading:1333044-Alleles,
pubmed-meshheading:1333044-Genetic Complementation Test,
pubmed-meshheading:1333044-Suppression, Genetic,
pubmed-meshheading:1333044-Plasmids,
pubmed-meshheading:1333044-Protein Kinases,
pubmed-meshheading:1333044-Restriction Mapping
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