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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1989-2-6
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pubmed:abstractText |
A substantial body of data, largely derived from study of cell extracts, indicates that protein synthesis in adenovirus-infected cells requires VA RNAI at late times of infection to prevent the activation of a protein kinase known as DAI, and the consequent phosphorylation of the alpha-subunit of initiation factor eIF-2. To verify this conclusion, we have measured the steady-state levels of eIF-2 alpha phosphorylation in cells infected with wild-type virus (Ad2) and a mutant that produces no VA RNAI (Ad5dl331). Consistent with the proposed mechanism, the alpha-subunit was very highly phosphorylated (approximately 90%) at late times of infection with Ad5dl331. Surprisingly, eIF-2 alpha phosphorylation also increased (to approximately 30%) at late times of infection with Ad2, suggesting that VA RNA and DAI might be involved in the selective translation of viral mRNA and the shut-off of host cell protein synthesis during the late phase. In agreement with this model, host protein synthesis shut-off is defective in cells expressing low levels of DAI.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Eukaryotic Initiation Factor-2,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Initiation Factors,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/eIF-2 Kinase
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0042-6822
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
168
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
112-8
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2909985-Adenoviruses, Human,
pubmed-meshheading:2909985-Autoradiography,
pubmed-meshheading:2909985-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:2909985-Eukaryotic Initiation Factor-2,
pubmed-meshheading:2909985-HeLa Cells,
pubmed-meshheading:2909985-Humans,
pubmed-meshheading:2909985-Immunoblotting,
pubmed-meshheading:2909985-Isoelectric Focusing,
pubmed-meshheading:2909985-Mutation,
pubmed-meshheading:2909985-Peptide Initiation Factors,
pubmed-meshheading:2909985-Phosphorylation,
pubmed-meshheading:2909985-Protein Biosynthesis,
pubmed-meshheading:2909985-Protein Kinases,
pubmed-meshheading:2909985-Proteins,
pubmed-meshheading:2909985-RNA, Viral,
pubmed-meshheading:2909985-eIF-2 Kinase
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pubmed:year |
1989
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pubmed:articleTitle |
Modification of protein synthesis initiation factors and the shut-off of host protein synthesis in adenovirus-infected cells.
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pubmed:affiliation |
Cold Spring Harbor Laboratory, New York 11724.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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