Abstract
The process of protein synthesis on ribosomes is promoted by soluble protein factors that act during the initiation, elongation and termination phases of translation (for reviews, see Moldave, 1985; Pain, 1986). A striking characteristic of these factors is that most of them bind GTP or GDP. Since the structure and mechanism of action of these proteins have been studied extensively for the past 20 years, considerable knowledge of their mechanisms of action has accummulated which may be relevant to understanding how G-proteins function in general. We are concerned here with one of the mammalian factors, initiation factor eIF2.
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References
Anthony, D.D., Dever, T.E., Abramson, R.D., Lobur, M., and Merrick, W.C., 1986, Affinity labeling of protein synthesis factors. Fed. Proc. 45:1768.
Clemens, M.J., Galpine, A., Austin, S.A., Panniers, R., Henshaw, E.C., Duncan, R., Hershey, J.W.B., and Pollard, J., 1987, Regulation of polypeptide chain initiation in CHO cells with a temperature-sensitive leucyl-tRNA synthetase: Changes in phosphorylation of initiation factor eIF-2 and in the activity of the guanine nucleotide exchange factor GEF. J. Biol. Chem. 262:767–771.
Colthurst, D.R., Campbell, D.G., and Proud, C.G., 1987, Structure and regulation of eukaryotic initiation factor eIF2. Sequence of the site in the a subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitor. Eur. J. Biochem. 166:357–363.
De Benedetti, A., and Baglioni, C., 1984, Inhibition of mRNA binding to ribosomes by localized activation of dsRNA-dependent protein kinase. Nature. 311:79–81.
Donahue, T.F., Cigan, A.M., Pabich, E.K. and Valavicius, B.C., 1988, Mutations at a zinc(II) finger motif in the eIF-20 gene in yeast alter translation initiation codon selection during the scanning process. Cell, in press.
Duncan, R., and Hershey, J.W.B., 1984, Heat-shock-induced translational alteractions in HeLa cells. J. Biol.Chem. 259:11882–11889.
Duncan, R., and Hershey, J.W.B., 1985, Regulation of initiation factors during translational repression caused by serum deprivation. J. Biol. Chem. 260:5493–5497.
Duncan, R.F., and Hershey, J.W.B., 1987, Translational repression by chemical inducers of the stress response occurs by different pathways. Arch. Biochem. Biophvs. 256:651–661.
Ernst, H., Duncan, R.F., and Hershey, J.W.B., 1987, Cloning and sequencing of complementary DNAs encoding the α-subunit of translational initiation factor eIF-2. J. Biol. Chem. 77:1286–1290.
Ernst, V., Baum, E.Z., and Reddy, P., 1982, in Heat Shock: from Bacteria to Man (Schlesinger, M.J., Ashburner, M., and Tissieres, A., eds.) pp. 215–225, Cold Spring Harbor Laboratory, NY.
Harbitz, I., and Hauge, J.G., 1979, Purification and properties of eIF-2 from pig liver. Methods Enzvmol. 60:240–246.
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.
Kaufman, R.J., and Murtha, P., 1987, Translational control mediated by eukaryotic initiation factor-2 is restricted to specific mRNAs in transfected cells. Molec. Cell. Biol. 7:1568–1571.
Kurzchalia, T.V., Bommer, V.A., Babkina, G.T., and Karpova, G.G., 1984, GTP interacts with the γ-subunit of eukaryotic initiation factor eIF-2. FEBS Lett. 175:313–316.
Moldave, K., 1985, Eukaryotic protein synthesis. Annu. Rev. Biochem. 54:1109–1149.
Ochoa, S., 1983, Regulation of protein synthesis in eukaryotes. Arch. Biochem. Biophvs. 223:325–349.
Pain, V.M., 1986, Initiation of protein synthesis in mammalian cells. Biochem. J. 235:625–637.
Pathak, V.K., Nielsen, P.J., Trachsel, H., and Hershey, J.W.B., 1988a, Structure of the ß subunit of translational initiation factor eIF-2. Cell, in press.
Pathak, V.K., Schindler, D., and Hershey, J.W.B., 1988b, Generation of a mutant form of protein synthesis initiation factor eIF-2 lacking the site of phosphorylation by eIF-2 kinases. Molec. Cell. Biol. 8:993–995.
Posorske, L.H., Cohn, M., Yanagisawa, N., and Auld, D.S., 1979, Methionyl-tRNA synthetase of Escherichia coli. A zinc metalloprotein. Biochim. Biophvs. Acta. 576:128–133.
Proud, C.G., 1986, Guanine nucleotides, protein phosphorylation and the control of translation. Trends Biochem. 11:73–77.
Rowlands, A.G., Panniers, R., and Henshaw, E.C., 1988, The catalytic mechanism of guanine nucleotide exchange factor action and competitive inhibition by phosphorylated eukaryotic initiation factor 2. J. Biol. Chem. 263:5526–5533.
Schneider, R.J., and Shenk, T., 1987, Impact of virus infection on host cell protein synthesis. Annu. Rev. Biochem. 56:317–332.
Stringer, E.A., Chaudhuri, A., and Maitra, U., 1979, Purified eukaryotic initiation factor 2 consists of two polypeptide chains of 48,000 and 38,000 daltons. J. Biol. Chem. 254:6845–6848.
Wettenhall, R.E.H., Kudlicki, W., Kramer, G., and Hardesty, B., 1986, The NH,-terminal sequence of the α and γ subunits of eukaryotic initiation factor 2 and the phosphorylation site for the heme regulated eIF-2α kinase. J. Biol. Chem. 261:12444–12447.
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Hershey, J.W.B., Pathak, V.K., Ernst, H., Hümbelin, M., Kaufman, R.J. (1989). The Structure and Regulation of Mammalian Initiation Factor eIF2. In: Bosch, L., Kraal, B., Parmeggiani, A. (eds) The Guanine — Nucleotide Binding Proteins. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-2037-2_14
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DOI: https://doi.org/10.1007/978-1-4757-2037-2_14
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