Modification of protein synthesis initiation factors and the shut-off of host protein synthesis in adenovirus-infected cells

O'Malley, R. P., Duncan, R. F., Hershey, J. W., Mathews, M. B. (January 1989) Modification of protein synthesis initiation factors and the shut-off of host protein synthesis in adenovirus-infected cells. Virology, 168 (1). pp. 112-8. ISSN 0042-6822

URL: http://www.ncbi.nlm.nih.gov/pubmed/2909985
DOI: 10.1016/0042-6822(89)90409-1

Abstract

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.

Item Type: Paper
Uncontrolled Keywords: Adenoviruses, Human/enzymology/genetics/*metabolism Autoradiography Electrophoresis, Polyacrylamide Gel Eukaryotic Initiation Factor-2 Hela Cells Humans Immunoblotting Isoelectric Focusing Mutation Peptide Initiation Factors/*metabolism Phosphorylation *Protein Biosynthesis Protein Kinases/analysis Proteins/*metabolism RNA, Viral/physiology Research Support, U.S. Gov't, P.H.S. eIF-2 Kinase
Subjects: organism description > virus > adenovirus
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein expression > phosphorylation
CSHL Authors:
Communities: CSHL labs
Depositing User: Gail Sherman
Date: January 1989
Date Deposited: 23 Jun 2017 20:16
Last Modified: 23 Jun 2017 20:16
Related URLs:
URI: http://repository.cshl.edu/id/eprint/34889

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