Purification and Characterization of mRNA Cap-Binding Protein from Drosophila melanogaster Embryos

LITERATURE CITED

• Abramson, R. D., K. S. Browning, T. E. Dever, T. G. Lawson, R. E. Thach, J. M. Ravel, and W. C. Merrick. 1988. Initiation factors that bind mRNA. A comparison of mammalian factors with wheat germ factors. J. Biol. Chem. 263:5462–5467.
   PubMed Web of Science ®Google Scholar
• Abramson, R. D., T. E. Dever, T. G. Lawson, B. K. Ray, R. E. Thach, and W. C. Merrick. 1987. The ATP-dependent interaction of eukaryotic initiation factors with mRNA. J. Biol. Chem. 262:3826–3832.
   PubMedGoogle Scholar
• Altmann, M., I. Edery, N. Sonenberg, and H. Trachsel. 1985. Purification and characterization of protein synthesis initiation factor eIF-4E from the yeast Saccharomyces cerevisiae. Biochemistry 24:6085–6089.
   PubMed Web of Science ®Google Scholar
• Altmann, M., C. Handschin, and H. Trachsel. 1987. mRNA cap-binding protein: cloning of the gene encoding protein synthesis initiation factor eIF-4E from Saccharomyces cerevisiae. Mol. Cell. Biol. 7:998–1003.
   PubMedGoogle Scholar
• Bergmann, J. E., and H. F. Lodish. 1979. Translation of capped and uncapped vesicular stomatitis virus and reovirus mRNAs. J. Biol. Chem. 254:459–468.
   PubMedGoogle Scholar
• Bonneau, A. M., and N. Sonenberg. 1987. Involvement of the 24-kDa cap-binding protein in regulation of protein synthesis in mitosis. J. Biol. Chem. 262:11134–11139.
   PubMedGoogle Scholar
• Bradford, M. M.. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248–254.
   PubMed Web of Science ®Google Scholar
• Brenner, C., N. Nakayama, M. Goebl, K. Tanaka, A. Toh-e, and K. Matsumoto. 1988. CDC33 encodes mRNA cap-binding protein eIF-4E of Saccharomyces cerevisiae. Mol. Cell. Biol. 8:3556–3559.
   PubMedGoogle Scholar
• Browning, K. S., S. R. Lax, and J. M. Ravel. 1987. Identification of two messenger RNA cap binding proteins in wheat germ. J. Biol. Chem. 262:11228–11232.
   PubMedGoogle Scholar
• Buckley, B., and E. Ehrenfeld. 1987. The cap-binding protein complex in uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 262:13599–13606.
   PubMedGoogle Scholar
• Duncan, R., S. C. Milburn, and J. W. B. Hershey. 1987. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. J. Biol. Chem. 262:380–388.
   PubMed Web of Science ®Google Scholar
• Edery, I., M. Hümbelin, A. Darveau, K. A. W. Lee, S. Milburn, J. W. B. Hershey, H. Trachsel, and N. Sonenberg. 1983. Involvement of eukaryotic initiation factor 4A in the cap recognition process. J. Biol. Chem. 258:11398–11403.
   PubMed Web of Science ®Google Scholar
• Etchinson, D., and S. Milburn. 1987. Separation of protein synthesis initiation factor eIF-4A from a p220-associated cap binding complex activity. Mol. Cell. Biochem. 76:15–25.
   PubMedGoogle Scholar
• Filipowicz, W., Y. Furuichi, J. M. Sierra, S. Muthukrishnan, A. J. Shatkin, and S. Ochoa. 1976. A protein binding the methylated 5′-terminal sequence, m7GpppN, of eukaryotic messenger RNA. Proc. Natl. Acad. Sci. USA 73:1559–1563.
   PubMed Web of Science ®Google Scholar
• Grifo, J. A., S. M. Tahara, M. A. Morgan, A. J. Shatkin, and W. C. Merrick. 1983. New initiation factor activity required for globin mRNA translation. J. Biol. Chem. 258:5804–5810.
   PubMedGoogle Scholar
• Hager, D. A., and R. R. Burgess. 1980. Elution of proteins from sodium dodecyl sulfate-polyacrylamide gels, removal of sodium dodecyl sulfate, and renaturation of enzymatic activity: results with sigma subunit of Escherichia coli RNA polymerase, wheat germ DNA topoisomerase, and other enzymes. Anal. Biochem. 109:76–86.
   PubMed Web of Science ®Google Scholar
• Hiremath, L. S., N. R. Webb, and R. E. Rhoads. 1985. Immunological detection of the messenger RNA cap-binding protein. J. Biol. Chem. 260:7843–7849.
   PubMed Web of Science ®Google Scholar
• Kozak, M.. 1986. Regulation of protein synthesis in virus-infected animal cells. Adv. Virus Res. 31:229–292.
   PubMed Web of Science ®Google Scholar
• Laemmli, U. K.. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (London) 227:680–685.
   PubMed Web of Science ®Google Scholar
• Lasko, P. F., and M. Ashburner. 1988. The product of the Drosophila gene vasa is very similar to eukaryotic initiation factor-4A. Nature (London) 335:611–617.
   PubMed Web of Science ®Google Scholar
• Lawson, T. G., M. H. Cladaras, B. K. Ray, K. A. Lee, R. D. Abramson, W. C. Merrick, and R. E. Thach. 1988. Discriminatory interaction of purified eukaryotic initiation factors 4F plus 4A with the 5′ ends of reovirus messenger RNAs. J. Biol. Chem. 263:7266–7276.
   PubMed Web of Science ®Google Scholar
• Lopo, A. C., S. MacMillan, and J. W. B. Hershey. 1988. Translational control in early sea urchin embryogenesis: initiation factor eIF-4F stimulates protein synthesis in lysates from unfertilized eggs of Strongylocentrotus purpuratus. Biochemistry 27:351–357.
   PubMedGoogle Scholar
• Maroto, F. G., and J. M. Sierra. 1988. Translational control in heat-shocked Drosophila embryos. Evidence for the inactivation of initiation factor(s) involved in the recognition of mRNA cap structure. J. Biol. Chem. 263:15720–15725.
   PubMedGoogle Scholar
• Mateu, M. G., and J. M. Sierra. 1987. Protein synthesis in Drosophila melanogaster embryos. Two mechanisms for guanine nucleotide exchange on eukaryotic initiation factor 2. Eur. J. Biochem. 165:507–513.
   PubMedGoogle Scholar
• Mateu, M. G., O. Vicente, and J. M. Sierra. 1987. Protein synthesis in Drosophila melanogaster embryos. Purification and characterization of polypeptide chain-initiation factor 2. Eur. J. Biochem. 162:221–229.
   PubMedGoogle Scholar
• Nielsen, P. J., and H. Trachsel. 1988. The mouse protein synthesis initiation factor 4A gene family includes two related functional genes which are differentially expressed. EMBO J. 7:2097–2105.
   PubMedGoogle Scholar
• Pain, V. M.. 1986. Initiation of protein synthesis in mammalian cells. Biochem. J. 235:625–637.
   PubMed Web of Science ®Google Scholar
• Palomo, C., and J. M. Sierra. 1988. Note on the activation of the heme-stabilized translational inhibitor of reticulocyte lysates by oxidized glutathione. Biochimie 70:827–831.
   PubMedGoogle Scholar
• Palomo, C., O. Vicente, J. M. Sierra, and S. Ochoa. 1985. Studies on the activation of the heme-stabilized translational inhibitor of reticulocyte lysates by oxidized glutathione and NADPH depletion. Arch. Biochem. Biophys. 239:497–507.
   PubMedGoogle Scholar
• Panniers, R., E. B. Stewart, W. C. Merrick, and E. C. Henshaw. 1985. Mechanism of inhibition of polypeptide chain initiation in heat-shocked Ehrlich cells involves reduction of eukaryotic initiation factor 4F activity. J. Biol. Chem. 260:9648–9653.
   PubMed Web of Science ®Google Scholar
• Pelletier, J., and N. Sonenberg. 1987. The involvement of mRNA secondary structure in protein synthesis. Biochem. Cell Biol. 65:576–581.
   PubMed Web of Science ®Google Scholar
• Ray, B. K., T. G. Lawson, J. C. Kramer, M. H. Cladaras, J. A. Grifo, R. D. Abramson, W. C. Merrick, and R. E. Thach. 1985. ATP-dependent unwinding of messenger RNA structure by eukaryotic initiation factors. J. Biol. Chem. 260:7651–7658.
   PubMed Web of Science ®Google Scholar
• Rhoads, R. E.. 1988. Cap recognition and the entry of mRNA into the protein synthesis initiation cycle. Trends Biochem. Sci. 13:52–56.
   PubMedGoogle Scholar
• Rychlik, W., L. L. Domier, P. R. Gardner, G. M. Hellmann, and R. E. Rhoads. 1987. Amino acid sequence of the mRNA cap-binding protein from human tissues. Proc. Natl. Acad. Sci. USA 84:945–949.
   PubMedGoogle Scholar
• Rychlik, W., P. R. Gardner, T. C. Vanaman, and R. E. Rhoads. 1986. Structural analysis of the messenger RNA cap-binding protein. J. Biol. Chem. 261:71–75.
   PubMedGoogle Scholar
• Rychlik, W., M. A. Russ, and R. E. Rhoads. 1987. Phosphorylation site of eukaryotic initiation factor 4E. J. Biol. Chem. 262:10434–10437.
   PubMed Web of Science ®Google Scholar
• Shatkin, A. J.. 1985. mRNA cap binding proteins: essential factors for initiating translation. Cell 40:223–224.
   PubMed Web of Science ®Google Scholar
• Sonenberg, N.. 1981. ATP/Mg2+-dependent crosslinking of cap binding proteins to the 5′ end of eukaryotic mRNA. Nucleic Acids Res. 9:1643–1656.
   PubMedGoogle Scholar
• Sonenberg, N.. 1987. Regulation of translation by poliovirus. Adv. Virus Res. 33:175–204.
   PubMedGoogle Scholar
• Sonenberg, N., M. A. Morgan, W. C. Merrick, and A. J. Shatkin. 1978. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5′-terminal cap in mRNA. Proc. Natl. Acad. Sci. USA 75:4843–4847.
   PubMed Web of Science ®Google Scholar
• Sonenberg, N., K. M. Ruprecht, S. M. Hecht, and A. J. Shatkin. 1979. Eukaryotic mRNA cap binding protein: purification by affinity chromatography on sepharose-coupled m7GDP. Proc. Natl. Acad. Sci. USA 76:4345–4349.
   PubMedGoogle Scholar
• Tahara, S. M., M. A. Morgan, and A. J. Shatkin. 1981. Two forms of purified m7G-cap binding protein with different effects on capped mRNA translation in extracts of uninfected and poliovirus-infected HeLa cells. J. Biol. Chem. 256:7691–7694.
   PubMedGoogle Scholar
• Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350–4354.
   PubMed Web of Science ®Google Scholar
• Voller, A., D. Bidwell, and A. Barlett. 1980. Enzyme-linked immunosorbent assay, p. 359. In N. Rose, and H. Friedman (ed.), Manual of clinical immunology, 2nd ed. American Society for Microbiology, Washington, D.C.
   Google Scholar
• Webb, N. R., R. V. J. Chari, G. Depillis, J. W. Kozarich, and R. E. Rhoads. 1984. Purification of the messenger RNA capbinding protein using a new affinity medium. Biochemistry 23:177–181.
   PubMed Web of Science ®Google Scholar
• Weber, L. A., E. D. Hickey, and C. Baglioni. 1978. Influence of potassium salt concentration and temperature on inhibition of mRNA translation by 7-methylguanosine 5′-monophosphate. J. Biol. Chem. 253:178–183.
   PubMedGoogle Scholar