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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
1993-9-7
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pubmed:abstractText |
Phosphorylation of eIF-2 alpha in Saccharomyces cerevisiae by the protein kinase GCN2 leads to inhibition of general translation initiation and a specific increase in translation of GCN4 mRNA. We isolated mutations in the eIF-2 alpha structural gene that do not affect the growth rate of wild-type yeast but which suppress the toxic effects of eIF-2 alpha hyperphosphorylation catalyzed by mutationally activated forms of GCN2. These eIF-2 alpha mutations also impair translational derepression of GCN4 in strains expressing wild-type GCN2 protein. All four mutations alter single amino acids within 40 residues of the phosphorylation site in eIF-2 alpha; however, three alleles do not decrease the level of eIF-2 alpha phosphorylation. We propose that these mutations alter the interaction between eIF-2 and its recycling factor eukaryotic translation initiation factor 2B (eIF-2B) in a way that diminishes the inhibitory effect of phosphorylated eIF-2 on the essential function of eIF-2B in translation initiation. These mutations may identify a region in eIF-2 alpha that participates directly in a physical interaction with the GCN3 subunit of eIF-2B.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-1348691,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-1448107,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-1739968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-1883206,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-1986242,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2005788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2038326,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2038327,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2188100,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2249755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2649894,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2659436,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-271968,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-2948954,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-3045517,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-3323810,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-6095062,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-6336730,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-8099443,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-8441423,
http://linkedlifedata.com/resource/pubmed/commentcorrection/8102207-8506384
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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 |
Aug
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pubmed:issn |
0027-8424
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
90
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7215-9
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8102207-Amino Acid Sequence,
pubmed-meshheading:8102207-Base Sequence,
pubmed-meshheading:8102207-Eukaryotic Initiation Factor-2,
pubmed-meshheading:8102207-Gene Expression Regulation, Fungal,
pubmed-meshheading:8102207-Genes, Suppressor,
pubmed-meshheading:8102207-Guanine Nucleotide Exchange Factors,
pubmed-meshheading:8102207-Molecular Sequence Data,
pubmed-meshheading:8102207-Oligodeoxyribonucleotides,
pubmed-meshheading:8102207-Peptide Chain Initiation, Translational,
pubmed-meshheading:8102207-Phosphorylation,
pubmed-meshheading:8102207-Protein-Serine-Threonine Kinases,
pubmed-meshheading:8102207-Proteins,
pubmed-meshheading:8102207-Saccharomyces cerevisiae,
pubmed-meshheading:8102207-Structure-Activity Relationship,
pubmed-meshheading:8102207-eIF-2 Kinase
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pubmed:year |
1993
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pubmed:articleTitle |
Mutations in the alpha subunit of eukaryotic translation initiation factor 2 (eIF-2 alpha) that overcome the inhibitory effect of eIF-2 alpha phosphorylation on translation initiation.
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pubmed:affiliation |
Section on Molecular Genetics of Lower Eukaryotes, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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