Skip to main content
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1973 Jul;70(7):2139–2144. doi: 10.1073/pnas.70.7.2139

Discrimination between Messenger Ribonucleic Acids by a Mammalian Translation Initiation Factor

U Nudel 1, B Lebleu 1, M Revel 1
PMCID: PMC433683  PMID: 4352974

Abstract

A factor from rabbit-reticulocyte ribosome, which stimulates by 5-fold initiation of hemoglobin mRNA translation in Krebs ascites cell extracts, was purified to homogeneity. The factor, a protein of about 65,000 molecular weight in sodium dodecyl sulfate, discriminates between various mRNAs: it stimulates translation of α globin mRNA and of tobacco mosaic virus RNA, but has only a small effect on β globin mRNA and no effect at all on Mengo virus RNA translation.

Keywords: reticulocyte initiation factors, hemoglobin synthesis, Krebs ascites extracts

Full text

PDF
2144

Selected References

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

  1. Conconi F., Rowley P. T., Del Senno L., Pontremoli S., Volpato S. Induction of -globin synthesis in the -thalassaemia of Ferrara. Nat New Biol. 1972 Jul 19;238(81):83–87. doi: 10.1038/newbio238083a0. [DOI] [PubMed] [Google Scholar]
  2. Crystal R. G., Nienhuis A. W., Prichard P. M., Picciano D., Elson N. A., Merrick W. C., Graf H., Shafritz D. A., Laycock D. G., Last J. A. Initiation of globin synthesis. FEBS Lett. 1972 Aug 15;24(3):310–314. doi: 10.1016/0014-5793(72)80379-x. [DOI] [PubMed] [Google Scholar]
  3. Falcoff E., Falcoff R., Lebleu B., Revel M. Interferon treatment inhibits Mengo RNA and haemoglobin mRNA translation in cell-free extracts of L cells. Nat New Biol. 1972 Nov 29;240(100):145–147. doi: 10.1038/newbio240145a0. [DOI] [PubMed] [Google Scholar]
  4. Groner Y., Pollack Y., Berissi H., Revel M. Characterization of cistron specific factors for the initiation of messenger RNA translation in E. coli. FEBS Lett. 1972 Mar 15;21(2):223–228. doi: 10.1016/0014-5793(72)80142-x. [DOI] [PubMed] [Google Scholar]
  5. Groner Y., Pollack Y., Berissi H., Revel M. Cistron specific translation control protein in Escherichia coli. Nat New Biol. 1972 Sep 6;239(88):16–19. doi: 10.1038/newbio239016a0. [DOI] [PubMed] [Google Scholar]
  6. Heywood S. M. Specificity of mRNA binding factor in eukaryotes. Proc Natl Acad Sci U S A. 1970 Dec;67(4):1782–1788. doi: 10.1073/pnas.67.4.1782. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Hsu W. T., Weiss S. B. Selective translation of T4 template RNA by ribosomes from T4-infected Escherichia coli. Proc Natl Acad Sci U S A. 1969 Sep;64(1):345–351. doi: 10.1073/pnas.64.1.345. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Huez G., Burny A., Marbaix G., Lebleu B. Release of messenger RNA from rabbit reticulocyte polyribosomes at low concentration of divalent cations. Biochim Biophys Acta. 1967;145(3):629–636. doi: 10.1016/0005-2787(67)90122-0. [DOI] [PubMed] [Google Scholar]
  9. Laemmli U. K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970 Aug 15;227(5259):680–685. doi: 10.1038/227680a0. [DOI] [PubMed] [Google Scholar]
  10. Lebleu B., Nudel U., Falcoff E., Prives C., Revel M. A comparison of the translation of Mengo virus RNA and globin mRNA in krebs ascites cell-free extracts. FEBS Lett. 1972 Sep 1;25(1):97–103. doi: 10.1016/0014-5793(72)80463-0. [DOI] [PubMed] [Google Scholar]
  11. Lee-Huang S., Ochoa S. Messenger discriminating species of initiation factor F3. Nat New Biol. 1971 Dec 22;234(51):236–239. doi: 10.1038/newbio234236a0. [DOI] [PubMed] [Google Scholar]
  12. Lee-Huang S., Ochoa S. Specific inhibitors of MS2 and late T4 RNA translation in E. coli. Biochem Biophys Res Commun. 1972 Oct 17;49(2):371–376. doi: 10.1016/0006-291x(72)90420-2. [DOI] [PubMed] [Google Scholar]
  13. Leibowitz R., Penman S. Regulation of protein synthesis in HeLa cells. 3. Inhibition during poliovirus infection. J Virol. 1971 Nov;8(5):661–668. doi: 10.1128/jvi.8.5.661-668.1971. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Lodish H. F. Alpha and beta globin messenger ribonucleic acid. Different amounts and rates of initiation of translation. J Biol Chem. 1971 Dec 10;246(23):7131–7138. [PubMed] [Google Scholar]
  15. Mathews M. B., Pragnell I. B., Osborn M., Arnstein H. R. Stimulation by reticulocyte initiation factors of protein synthesis in a cell-free system from Krebs II ascites cells. Biochim Biophys Acta. 1972 Nov 16;287(1):113–123. doi: 10.1016/0005-2787(72)90335-8. [DOI] [PubMed] [Google Scholar]
  16. Mathews M., Korner A. Mammalian cell-free protein synthesis directed by viral ribonucleic acid. Eur J Biochem. 1970 Dec;17(2):328–338. doi: 10.1111/j.1432-1033.1970.tb01170.x. [DOI] [PubMed] [Google Scholar]
  17. McDowell M. J., Joklik W. K., Villa-Komaroff L., Lodish H. F. Translation of reovirus messenger RNAs synthetesized in vitro into reovirus polypeptides by several mammalian cell-free extracts. Proc Natl Acad Sci U S A. 1972 Sep;69(9):2649–2653. doi: 10.1073/pnas.69.9.2649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Metafora S., Terada M., Dow L. W., Marks P. A., Bank A. Increased efficiency of exogenous messenger RNA translation in a Krebs ascites cell lysate. Proc Natl Acad Sci U S A. 1972 May;69(5):1299–1303. doi: 10.1073/pnas.69.5.1299. [DOI] [PMC free article] [PubMed] [Google Scholar]
  19. Pollack Y., Groner Y., Aviv(Greenshpan) H., Revel M. Role of initiation factor B (F3) in the preferential translation of T4 late messenger RNA in T4 infected E. Coli. FEBS Lett. 1970 Aug 17;9(4):218–221. doi: 10.1016/0014-5793(70)80359-3. [DOI] [PubMed] [Google Scholar]
  20. Rourke A. W., Heywood S. M. Myosin synthesis and specificity of eukaryotic initiation factors. Biochemistry. 1972 May 23;11(11):2061–2066. doi: 10.1021/bi00761a010. [DOI] [PubMed] [Google Scholar]
  21. Sampson J., Borghetti A. F. Translation of rabbit globin mRNA. Nat New Biol. 1972 Aug 16;238(85):200–202. doi: 10.1038/newbio238200a0. [DOI] [PubMed] [Google Scholar]
  22. Tomkins G. M., Gelehrter T. D., Granner D., Martin D., Jr, Samuels H. H., Thompson E. B. Control of specific gene expression in higher organisms. Expression of mammalian genes may be controlled by repressors acting on the translation of messenger RNA. Science. 1969 Dec 19;166(3912):1474–1480. doi: 10.1126/science.166.3912.1474. [DOI] [PubMed] [Google Scholar]
  23. Wigle D. T., Smith A. E. Specificity in initiation of protein synthesis in a fractionated mammalian cell-free system. Nat New Biol. 1973 Apr 4;242(118):136–140. doi: 10.1038/newbio242136a0. [DOI] [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES