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. 1987 Mar;7(3):1293–1295. doi: 10.1128/mcb.7.3.1293

Initiation factor protein modifications and inhibition of protein synthesis.

R F Duncan, J W Hershey
PMCID: PMC365207  PMID: 3561417

Abstract

The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. COLOMBO B., FELICETTI L., BAGLIONI C. INHIBITION OF PROTEIN SYNTHESIS BY CYCLOHEXIMIDE IN RABBIT RETICULOCYTES. Biochem Biophys Res Commun. 1965 Feb 3;18:389–395. doi: 10.1016/0006-291x(65)90719-9. [DOI] [PubMed] [Google Scholar]
  2. Cassel D., Rothenberg P., Zhuang Y. X., Deuel T. F., Glaser L. Platelet-derived growth factor stimulates Na+/H+ exchange and induces cytoplasmic alkalinization in NR6 cells. Proc Natl Acad Sci U S A. 1983 Oct;80(20):6224–6228. doi: 10.1073/pnas.80.20.6224. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. De Benedetti A., Baglioni C. Activation of hemin-regulated initiation factor-2 kinase in heat-shocked HeLa cells. J Biol Chem. 1986 Jan 5;261(1):338–342. [PubMed] [Google Scholar]
  4. Duncan R., Hershey J. W. Evaluation of isoelectric focusing running conditions during two-dimensional isoelectric focusing/sodium dodecyl sulfate-polyacrylamide gel electrophoresis: variation of gel patterns with changing conditions and optimized isoelectric focusing conditions. Anal Biochem. 1984 Apr;138(1):144–155. doi: 10.1016/0003-2697(84)90783-8. [DOI] [PubMed] [Google Scholar]
  5. Duncan R., Hershey J. W. Heat shock-induced translational alterations in HeLa cells. Initiation factor modifications and the inhibition of translation. J Biol Chem. 1984 Oct 10;259(19):11882–11889. [PubMed] [Google Scholar]
  6. Duncan R., Hershey J. W. Identification and quantitation of levels of protein synthesis initiation factors in crude HeLa cell lysates by two-dimensional polyacrylamide gel electrophoresis. J Biol Chem. 1983 Jun 10;258(11):7228–7235. [PubMed] [Google Scholar]
  7. Duncan R., Hershey J. W. Regulation of initiation factors during translational repression caused by serum depletion. Covalent modification. J Biol Chem. 1985 May 10;260(9):5493–5497. [PubMed] [Google Scholar]
  8. Duncan R., Milburn S. C., Hershey J. W. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F. J Biol Chem. 1987 Jan 5;262(1):380–388. [PubMed] [Google Scholar]
  9. Etchison D., Milburn S. C., Edery I., Sonenberg N., Hershey J. W. Inhibition of HeLa cell protein synthesis following poliovirus infection correlates with the proteolysis of a 220,000-dalton polypeptide associated with eucaryotic initiation factor 3 and a cap binding protein complex. J Biol Chem. 1982 Dec 25;257(24):14806–14810. [PubMed] [Google Scholar]
  10. Farrell P. J., Balkow K., Hunt T., Jackson R. J., Trachsel H. Phosphorylation of initiation factor elF-2 and the control of reticulocyte protein synthesis. Cell. 1977 May;11(1):187–200. doi: 10.1016/0092-8674(77)90330-0. [DOI] [PubMed] [Google Scholar]
  11. Flaim K. E., Peavy D. E., Everson W. V., Jefferson L. S. The role of amino acids in the regulation of protein synthesis in perfused rat liver. I. Reduction in rates of synthesis resulting from amino acid deprivation and recovery during flow-through perfusion. J Biol Chem. 1982 Mar 25;257(6):2932–2938. [PubMed] [Google Scholar]
  12. Grainger J. L., Winkler M. M., Shen S. S., Steinhardt R. A. Intracellular pH controls protein synthesis rate in the sea urchine egg and early embryo. Dev Biol. 1979 Feb;68(2):396–406. doi: 10.1016/0012-1606(79)90213-6. [DOI] [PubMed] [Google Scholar]
  13. Grifo J. A., Tahara S. M., Morgan M. A., Shatkin A. J., Merrick W. C. New initiation factor activity required for globin mRNA translation. J Biol Chem. 1983 May 10;258(9):5804–5810. [PubMed] [Google Scholar]
  14. Hershko A., Mamont P., Shields R., Tomkins G. M. "Pleiotypic response". Nat New Biol. 1971 Aug;232(33):206–211. [PubMed] [Google Scholar]
  15. Jagus R., Anderson W. F., Safer B. The regulation of initiation of mammalian protein synthesis. Prog Nucleic Acid Res Mol Biol. 1981;25:127–185. doi: 10.1016/s0079-6603(08)60484-5. [DOI] [PubMed] [Google Scholar]
  16. Johnson T. C., Holland J. J. Ribonucleic acid and protein synthesis in mitotic HeLa cells. J Cell Biol. 1965 Dec;27(3):565–574. doi: 10.1083/jcb.27.3.565. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Koch F., Koch G. Reversible inhibition of macromolecular synthesis in HeLa cells by ethanol. Res Commun Chem Pathol Pharmacol. 1974 Oct;9(2):291–298. [PubMed] [Google Scholar]
  18. Matts R. L., London I. M. The regulation of initiation of protein synthesis by phosphorylation of eIF-2(alpha) and the role of reversing factor in the recycling of eIF-2. J Biol Chem. 1984 Jun 10;259(11):6708–6711. [PubMed] [Google Scholar]
  19. Moldave K. Eukaryotic protein synthesis. Annu Rev Biochem. 1985;54:1109–1149. doi: 10.1146/annurev.bi.54.070185.005333. [DOI] [PubMed] [Google Scholar]
  20. Moolenaar W. H., Tsien R. Y., van der Saag P. T., de Laat S. W. Na+/H+ exchange and cytoplasmic pH in the action of growth factors in human fibroblasts. Nature. 1983 Aug 18;304(5927):645–648. doi: 10.1038/304645a0. [DOI] [PubMed] [Google Scholar]
  21. Pain V. M. Initiation of protein synthesis in mammalian cells. Biochem J. 1986 May 1;235(3):625–637. doi: 10.1042/bj2350625. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Robbins E., Pederson T., Klein P. Comparison of mitotic phenomena and effects induced by hypertonic solutions in HeLa cells. J Cell Biol. 1970 Feb;44(2):400–416. doi: 10.1083/jcb.44.2.400. [DOI] [PMC free article] [PubMed] [Google Scholar]
  23. Saborio J. L., Koch G. Reversible inhibition of protein synthesis in HeLa cells by dimethylsulfoxide. J Biol Chem. 1973 Dec 25;248(24):8343–8347. [PubMed] [Google Scholar]
  24. Safer B., Jagus R., Crouch D. Indirect inactivation of eukaryotic initiation factor 2 in reticulocyte lysate by selenite. J Biol Chem. 1980 Jul 25;255(14):6913–6917. [PubMed] [Google Scholar]
  25. Samuel C. E., Duncan R., Knutson G. S., Hershey J. W. Mechanism of interferon action. Increased phosphorylation of protein synthesis initiation factor eIF-2 alpha in interferon-treated, reovirus-infected mouse L929 fibroblasts in vitro and in vivo. J Biol Chem. 1984 Nov 10;259(21):13451–13457. [PubMed] [Google Scholar]
  26. Vernie L. N., Bont W. S., Ginjaar H. B., Emmelot P. Elongation factor 2 as the target of the reaction product between sodium selenite and glutathione (GSSeSG) in the inhibiting of amino acid incorporation in vitro. Biochim Biophys Acta. 1975 Dec 19;414(3):283–292. doi: 10.1016/0005-2787(75)90167-7. [DOI] [PubMed] [Google Scholar]

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