Translational Control Mediated by Eucaryotic Initiation Factor-2 Is Restricted to Specific mRNAs in Transfected Cells

LITERATURE CITED

• Blobel, G. 1985. Gene gating: a hypothesis. Proc. Natl. Acad. Sci. USA 82:8527–8529.
   PubMed Web of Science ®Google Scholar
• Chirgwin, J. M., A. E. Przybyla, R. J. MacDonald, and W. J. Rutter. 1979. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18:5294–5299.
   PubMed Web of Science ®Google Scholar
• De Benedetti, A., and C. Baglioni. 1983. Phosphorylation of initiation factor eIF-2α, binding of mRNA to 48 S complexes, and its reutilization in initiation of protein synthesis. J. Biol. Chem. 258:14556–14562.
   PubMedGoogle Scholar
• De Benedetti, A., and C. Baglioni. 1984. Inhibition of mRNA binding to ribosomes by localized actiation of dsRNA-dependent protein kinase. Nature (London) 311:79–81.
   PubMedGoogle Scholar
• Derman, E., K. Krauter, L. Walling, C. Weinberger, M. Ray, and J. R. DarnellJr, . 1981. Transcriptional control in the production of liver-specific mRNAs. Cell 23:731–739.
   PubMed Web of Science ®Google Scholar
• Jagus, R., W. F. Anderson, and B. Safer. 1981. The regulation of initiation of mammalian protein synthesis. Prog. Nucleic Acid Res. Mol. Biol. 25:127–185.
   PubMedGoogle Scholar
• Kaufman, R. J. 1985. Identification of the components necessary for adenovirus translational control and their utilization in cDNA expression vectors. Proc. Natl. Acad. Sci. USA 82:689–693.
   PubMed Web of Science ®Google Scholar
• Kaufman, R. J., J. R. Bertino, and R. T. Schimke. 1978. Quantitation of dihydrofolate reductase in individual parental and methotrexate-resistant murine cells. J. Biol. Chem. 253:5852–5860.
   PubMed Web of Science ®Google Scholar
• Kaufman, R. J., P. Murtha, D. E. Ingolia, C.-Y. Yeung, and R. E. Kellems. 1986. Selection and amplification of heterologous genes encoding adenosine deaminase in mammalian cells. Proc. Natl. Acad. Sci. USA 83:3136–3140.
   PubMedGoogle Scholar
• Kaufman, R. J., and P. A. Sharp. 1982. Construction of a modular dihydrofolate reductase cDNA gene: analysis of signals utilized for efficient expression. Mol. Cell. Biol. 2:1304–1319.
   PubMed Web of Science ®Google Scholar
• Kitajewski, J., R. J. Schneider, B. Safer, S. M. Munemitsu, C. E. Samuel, B. Thimmappaya, and T. Shenk. 1986. Adenovirus VAI RNA antagonizes the antiviral action of interferon by preventing activation of the interferon-induced eIF2 alpha kinase. Cell 45:195–200.
   PubMed Web of Science ®Google Scholar
• Lebleu, B., G. C. Sen, S. Shaila, B. Cabrer, and P. Lengrel. 1976. Interferon, double-stranded RNA and protein phosphorylation. Proc. Natl. Acad. Sci. USA 73:3107–3111.
   PubMed Web of Science ®Google Scholar
• Luthman, H., and G. Magnusson. 1983. High efficiency polyoma DNA transfection of chloroquine treated cells. Nucleic Acids Res. 11:1295–1308.
   PubMed Web of Science ®Google Scholar
• Mathews, M. B. (ed.). 1986. Translation control. Current communications in molecular biology. Cold Spring Harbor Laboratory, Cold Spring Harbor, N.Y.
   Google Scholar
• Ochoa, S. 1983. Regulation of protein synthesis in eukaryotes. Arch. Biochem. Biophys. 223:325–349.
   PubMedGoogle Scholar
• O'Malley, R. P., T. M. Mariano, J. Siekierka, and M. B. Mathews. 1986. A mechanism for the control of protein synthesis by adenovirus VA RNA1. Cell 44:391–400.
   PubMedGoogle Scholar
• Reichel, P. A., W. C. Merrick, J. Siekierka, and M. Mathews. 1985. Regulation of a protein synthesis initiation factor by adenovirus associated RNA I. Nature (London) 313:196–200.
   PubMedGoogle Scholar
• Roberts, W. K., A. Hovanessian, R. E. Brown, M. J. Clemens, and I. M. Kerr. 1976. Interferon-mediated protein kinase and low molecular-weight inhibitor of protein synthesis. Nature (London) 264:477–480.
   PubMed Web of Science ®Google Scholar
• Safer, B. 1983. 2B or not 2B: regulation of the catalytic utilization of eIF-2. Cell 33:7–8.
   PubMed Web of Science ®Google Scholar
• Samuel, C. E., D. A. Farris, and D. A. Eppstein. 1977. Mechanism of interferon action. Kinetics of interferon action in mouse L929 cells: translational inhibition, protein phosphorylation, and mRNA phosphorylation and degradation. Virology 83:56–71.
   PubMedGoogle Scholar
• Schneider, R. J., B. Safer, S. M. Munemitsu, C. E. Samuel, and T. Shenk. 1985. Adenovirus VA RNAI prevents phosphorylation of the eukaryotic initiation factor 2 subunit subsequent to infection. Proc. Natl. Acad. Sci. USA 82:4321–4325.
   PubMedGoogle Scholar
• Schneider, R. J., C. Weinberger, and T. Shenk. 1984. Adenovirus VAI RNA facilitated the initiation of translation in virus-infected cells. Cell 37:291–298.
   PubMedGoogle Scholar
• Siekierka, J., T. M. Mariano, P. A. Reichel, and M. B. Mathews. 1985. Translational control by adenovirus: lack of virus associated RNAI during adenovirus infection results in phosphorylation of initiation factor eIF-2 and inhibition of protein synthesis. Proc. Natl. Acad. Sci. USA 82:1959–1963.
   PubMedGoogle Scholar
• Sompayrac, L. M., and K. J. Dana. 1981. Efficient infection of monkey cells with DNA of simian virus 40. Proc. Natl. Acad. Sci. USA 78:7575–7578.
   PubMed Web of Science ®Google Scholar
• Svensson, C., and G. Akusjärvi. 1984. Adenovirus VA RNAI: a positive regulator of mRNA translation. Mol. Cell. Biol. 4:736–742.
   PubMedGoogle Scholar
• Svensson, C., and G. Akusjärvi. 1985. Adenovirus VA RNAI mediates a translational stimulation which is not restricted to the viral mRNAs. EMBO J. 4:957–964.
   PubMedGoogle Scholar
• Thimmappaya, B., C. Weinberger, R. J. Schneider, and T. Shenk. 1982. Adenovirus VA RNAI is required for efficient translation of viral mRNA at late times after infection. Cell 31:543–551.
   PubMedGoogle Scholar
• Thomas, P. 1980. Hybridization of denatured RNA and small DNA fragments transferred to nitrocellulose. Proc. Natl. Acad. Sci. USA 77:5201–5205.
   PubMed Web of Science ®Google Scholar
• Wong, G. G., J. S. Witek, P. A. Temple, K. M. Wilkens, A. C. Leary, D. P. Lexenberg, S. S. Jones, E. L. Brown, R. M. Kay, E. C. Orr, C. S. Shoemaker, D. W. Golde, R. J. Kaufman, R. M. Hewick, E. A. Wang, and S. C. Clark. 1985. Human GM-CSF: molecular cloning of the complementary DNA and purification of the natural and recombinant proteins. Science 228:810–815.
   PubMed Web of Science ®Google Scholar
• Yeung, C.-Y., D. E. Ingolia, D. B. Roth, C. Shoemaker, M. R. Al-Ubaili, J.-Y. Yen, C. Ching, C. Bobonis, R. J. Kaufman, and R. E. Kellems. 1985. Identification of functional murine adenosine deaminase cDNA clones by complementation in Escherichia coli. J. Biol. Chem. 260:10229–10307.
   Google Scholar
• Zilberstein, A., P. Federmann, L. Schulman, and M. Revel. 1976. Specific phosphorylation of a pretein associated with ribosomes of interferon-treated mouse L cells. FEBS Lett. 68:119–124.
   PubMedGoogle Scholar