Skip to main content
SpringerLink
Log in

Initiation of Translation

  • Chapter
Book cover Ribosomes

Part of the book series: Cellular Organelles ((CORG))

  • 205 Accesses

Abstract

The vacant ribosomal particles after termination may be again involved in translation. Several mechanisms of initiation of translation of a new message, or reinitiation of translation of the next coding sequence of the same polycistronic mRNA (in prokaryotes), or reinitiation of translation of the same monocistronic mRNA (in eukaryotes) by vacant post-termination ribosomes have evolved in living matter.

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 84.99
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 109.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Adams, J. M. (1968) On the release of the formyl group from nascent protein, J. Mol. Biol. 33:571–589.

    Article  PubMed  CAS  Google Scholar 

  • Bag, J. (1991) mRNA and mRNP, in Translation in Eukaryotes (H. Trachsel, ed.), pp. 71–96, CRC Press, Boca Raton, Ann Arbor, Boston, London.

    Google Scholar 

  • Basavappa, R., and Sigler, P. B. (1991) The 3 Å crystal structure of yeast initiator tRNA: functional implications in initiator/elongator discrimination, EMBO J. 10:3105–3111.

    PubMed  CAS  Google Scholar 

  • Biou, V., Shu, F., and Ramakrishnan, V. (1995) X-ray crystallography shows that translational initiation factor IF3 consists of two compact α/β domains linked by an α-helix, EMBO J. 14:4056–4064.

    PubMed  CAS  Google Scholar 

  • Capecchi, M. R. (1966) Initiation of E. coli proteins, Proc. Natl. Acad. Sci. USA 55:1517–1524.

    Article  PubMed  CAS  Google Scholar 

  • Clark, B. F. G, and Marcker, K. A. (1966) The role of N-formyl-methionyl-sRNA in protein biosynthesis, J. Mol. Biol. 17:394–406.

    Article  PubMed  CAS  Google Scholar 

  • Danthinne, X., Seurinck, J., Meulewaeter, F., van Montagu, M., and Cornelissen, M. (1993) The 3′ untranslated region of satellite tobacco necrosis virus RNA stimulates translation in vitro, Mol. Cell. Biol. 13:3340–3349.

    PubMed  CAS  Google Scholar 

  • de Smit, M. H., and van Duin, J. (1990) Control of prokaryotic translational initiation by mRNA secondary structure, Progr. Nucleic Acid Bes. Mol. Biol. 38:1–35.

    Article  Google Scholar 

  • Dyson, M. R., Mandal, N., and RajBhandary, U. L. (1993) Relationship between the structure and function of Escherichia coli initiator tRNA, Biochimie 75:1051–1060.

    Article  PubMed  CAS  Google Scholar 

  • Ehrenfeld, E. (1996) Initiation of translation by picornavirus RNAs, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.) pp. 549–574, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Forster, C., Chakraburtty, K., and Sprinzl, M. (1993) Discrimination between initiation and elongation of protein biosynthesis in yeast: identity assured by a nucleotide modification in the initiator tRNA, Nucleic Acids Bes. 21:5679–5683.

    Article  CAS  Google Scholar 

  • Gallie, D. R., Feder, J. N., Schimke, R. T, and Walbot, V. (1991) Functional analysis of the tobacco mosaic virus tRNA-like structure in cytoplasmic gene regulation, Nucleic Acids Bes. 19:5031–5036.

    Article  CAS  Google Scholar 

  • Gallie, D. R., and Walbot, V. (1990) RNA pseudoknot domain of tobacco mosaic virus can functionally substitute for a poly(A) tail in plant and animal cells, Genes and Develop. 4:1149–1157.

    Article  CAS  Google Scholar 

  • Garcia, C., Fortier, P.-L., Blanquet, S., Lallemand, J.-Y., and Dardel, F. (1995) Solution structure of the ribosome-binding domain of E. coli translation initiation factor IF3. Homology with the U1A protein of the eukaryotic spliceosome, J. Mol. Biol. 254:247–259.

    Article  PubMed  CAS  Google Scholar 

  • Grens, A., and Scheffler, I. E. (1990) The 5′-and 3′-untranslated regions of ornithine decarboxylase mRNA affect the translational efficiency, J. Biol. Chem. 265:11810–11816.

    PubMed  CAS  Google Scholar 

  • Gualerzi, C. O., La Teana, A., Spurio, R., Canonaco, M. A., Severini, M., and Pon, C. L. (1990) Initiation of protein synthesis in Procaryotes: Recognition of mRNA by ribosomes and molecular basis for the function of initiation factors, in The Bibosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 281–291, ASM Press, Washington, DC.

    Google Scholar 

  • Gualerzi, C., Pon, C. L., Pawlik, R. T., Canonaco, M. A., Pace, M., and Wintermeyer, W. (1986) Role of the initiation factors in Escherichia coli translational initiation, in Structure, Function and Genetics of Bibosomes (B. Hardesty and G. Kramer, eds.), pp. 621–641, Springer Verlag, New York.

    Chapter  Google Scholar 

  • Hartz, D., McPheeters, D. S., and Gold, L. (1990) From polynucleotide to natural mRNA translation initiation: Function of Escherichia coli initiation factors, in The Bibosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 275–280, ASM Press, Washington, DC.

    Google Scholar 

  • Ivanov, P. A., Karpova, O. V., Skulachev, M. V., Tomashevskaya, O. L., Rodionova, N. P., Dorokhov, Yu. L., and Atabekov, J. G. (1997) A tobamovirus genome that contains an internal ribosome entry site functional in vitro, Virology 232:32–43.

    Article  PubMed  CAS  Google Scholar 

  • Jackson, R. J. (1996) A comparative view of initiation site selection mechanisms, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 71–112, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Jacobson, A. (1996) Poly(A) metabolism and translation: The closed-loop model, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 451–480, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Kozak, M. (1978) How do eucaryotic ribosomes select initiation regions in messenger RNA?, Cell 15:1109–1123.

    Article  PubMed  CAS  Google Scholar 

  • Kozak, M. (1980) Role of ATP in binding and migration of 40S ribosomal subunits, Cell 22:459–467.

    Article  PubMed  CAS  Google Scholar 

  • Kozak, M. (1981) Possible role of flanking nucleotides in recognition of the AUG initiator codon by eukaryotic ribosomes, Nucleic Acids Res. 9:5233–5252.

    Article  PubMed  CAS  Google Scholar 

  • Kozak, M. (1983) Comparison of initiation of protein synthesis in prokaryotes, eukaryotes and organelles, Microbiol. Rev. 47:1–45.

    PubMed  CAS  Google Scholar 

  • Kozak, M. (1989a) Context effects and inefficient initiation at non-AUG codon in eukaryotic cell-free translation systems, Mol. Cell. Biol. 9:5073–5080.

    PubMed  CAS  Google Scholar 

  • Kozak, M. (1989b) The scanning model for translation: An update, J. Cell. Biol. 108:229–241.

    Article  PubMed  CAS  Google Scholar 

  • Leathers, V., Tanguay, R., Kobayashi, M., and Gallie, D. R. (1993) A phylogenetically conserved sequence within viral 3′ untranslated RNA pseudoknots regulates translation, Mol. Cell. Biol. 13:5331–5347.

    PubMed  CAS  Google Scholar 

  • Macejak, D. G., and Sarnow, P. (1991) Internal initiation of translation mediated by the 5′ leader of a cellular mRNA, Nature 353:90–94.

    Article  PubMed  CAS  Google Scholar 

  • Maitra, M., Stringer, E. A., and Chaudhuri, A. (1982) Initiation factors in protein biosynthesis. Annu. Rev. Biochem. 51:869–900.

    Article  PubMed  CAS  Google Scholar 

  • Manzella, J. M., and Blackshear, P. J. (1990) Regulation of rat ornithine decarboxylase mRNA translation by its 5′-untranslated region, J. Biol. Chem. 265:11817–11822.

    PubMed  CAS  Google Scholar 

  • Marcker, K., and Sanger, F. (1964) N-formyl-methionyl-sRNA, J. Mol. Biol. 8:835–840.

    Article  PubMed  CAS  Google Scholar 

  • McCarthy, J. E. G., and Brimacombe, R. (1994) Prokaryotic translation: the interactive pathway leading to initiation, Trends Genet. 10:402–407.

    Article  PubMed  CAS  Google Scholar 

  • McCarthy, J. E. G., and Gualerzi, C. (1990) Translational control of prokaryotic gene expression, Trends Genet. 6:78–85.

    Article  PubMed  CAS  Google Scholar 

  • Meerovitch, K., Sonenberg, N., and Pelletier, J. (1991) The translation of picornaviruses, in Translation in Eukaryotes (H. Trachsel, ed.), pp. 273–292, CRC Press, Boca Raton, Ann Arbor, Boston, London.

    Google Scholar 

  • Merrick, W. C. (1992) Mechanism and regulation of eukaryotic protein synthesis, Microbial Reviews 56:291–315.

    CAS  Google Scholar 

  • Merrick, W. C., and Hershey, J. W. B. (1996) The pathway and mechanism of eukaryotic protein synthesis, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 31–70, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Munroe, D., and Jacobson, A. (1990) Poly(A) is a 3′ enhancer of translational initiation, in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 299–305, ASM Press, Washington, DC.

    Google Scholar 

  • Oh, S.-K., Scott, M. P., and Sarnow, P. (1992) Homeotic gene Antennapedia mRNA contains 5′-non-coding sequences that confer translational initiation by internal ribosome binding, Genes and Develop. 6:1643–1653.

    Article  CAS  Google Scholar 

  • Pestova, T. V., Hellen, C. U. T., and Shatsky, I. N. (1996) Canonical eukaryotic initiation factors determine initiation of translation by internal ribosomal entry, Mol. Cell. Biol. 16:6859–6869.

    PubMed  CAS  Google Scholar 

  • Pilipenko, E. V., Gmyl, A. P., Maslova, S. V., Belov, G. A., Sinyakov, A. N., Huang, M., Brown, T. D. K., and Agol, V. I. (1994) Starting window, a distinct element in the cap-independent internal initiation of translation on picornaviral RNA, J. Mol. Biol. 241:398–414.

    Article  PubMed  CAS  Google Scholar 

  • Pilipenko, E. V., Gmyl, A. P., Maslova, S. V., Svitkin, Yu. V., Sinyakov, A. N., and Agol, V. I. (1992) Prokaryotic-like cis elements in the cap-independent internal initiation of translation on picornavirus RNA, Cell 68:119–131.

    Article  PubMed  CAS  Google Scholar 

  • Preobrazhensky, A. A., and Spirin, A. S. (1978) Informosomes and their protein components: The present state of knowledge, Progr. Nucleic Acid Res. Mol. Biol. 21:1–38.

    Article  CAS  Google Scholar 

  • Rhoads, R. E. (1991) Initiation: mRNA and 60S subunit binding, in Translation in Eukaryotes (H. Trachsel, ed.), pp. 109–148, CRC Press, Boca Raton, Ann Arbor, Boston, London.

    Google Scholar 

  • Sachs, A. (1990) The role of poly(A) in the translation and stability of mRNA, Curr. Opin. Cell Biol. 2:1092–1098.

    Article  PubMed  CAS  Google Scholar 

  • Shine, J., and Dalgarno, L. (1974) The 3′-terminal sequence of Escherichia coli 16S ribosomal RNA: Complementarity to nonsense triplets and ribosome binding sites, Proc. Natl. Acad. Sci. USA 71:1342–1346.

    Article  PubMed  CAS  Google Scholar 

  • Smith, A. E., and Marcker, K. A. (1970) Cytoplasmic methionine transfer RNAs from eukaryotes, Nature 226:607–610.

    Article  PubMed  CAS  Google Scholar 

  • Sonenberg, N. (1991) Picornavirus RNA translation continues to surprise, Trends Genet. 7:105–106.

    Article  PubMed  CAS  Google Scholar 

  • Spirin, A. S. (1994) Storage of messenger RNA in eukaryotes: Envelopment with protein, translational barrier at 5′ side, or conformational masking by 3′ side?, Mol. Reprod. Develop. 38:107–117.

    Article  CAS  Google Scholar 

  • Spirin, A. S. (1996) Masked and translatable messenger ribonucleoproteins in higher eukaryotes, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 319–334, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Steitz, J. A. (1980) RNA-RNA interactions during polypeptide chain initiation, in Ribosomes: Structure, Function, and Genetics (G. Chambliss, G. R. Craven, J. Davies, K. Davis, L. Kahan, and M. Nomura, eds.), pp. 479–495, University Park Press, Baltimore.

    Google Scholar 

  • Stormo, G. D. (1986) Translation initiation, in Maximizing Gene Expression (W. Reznikoff and L. Gold, eds.), pp. 195–224, Butterworths, Boston, London.

    Google Scholar 

  • Timmer, R. T, Benkowski, L. A., Schodin, D., Lax, S. R., Metz, A. M., Ravel, J. M., and Browning, K. S. (1993) The 5′ and 3′ untranslated regions of satellite tobacco necrosis virus RNA affect translational efficiency and dependence on 5′ cap structure, J. Biol. Chem. 268:9504–9510.

    PubMed  CAS  Google Scholar 

  • Trachsel, H. (1996) Binding of initiator methionyl-tRNA to ribosomes, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 113–138, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Van Knippenberg, P. H. (1990) Aspects of translation initiation in Escherichia coli, in The Ribosome: Structure, Function, and Evolution (W. E. Hill, A. Dahlberg, R. A. Garrett, P. B. Moore, D. Schlessinger, and J. R. Warner, eds.), pp. 265–274, ASM Press, Washington, DC.

    Google Scholar 

  • Varshney, U., Lee, C. P., and RajBhandary, U. L. (1993) From elongator tRNA to initiator tRNA, Proc. Natl. Acad. Sci. USA 90:2305–2309.

    Article  PubMed  CAS  Google Scholar 

  • Voorma, H. O. (1991) Initiation: Met-tRNA binding, in Translation in Eukaryotes (H. Trachsel, ed.), pp. 97–108, CRC Press, Boca Raton.

    Google Scholar 

  • Voorma, H. O. (1996) Control of translation initiation in prokaryotes, in Translational Control (J. W. B. Hershey, M. B. Matthews, and N. Sonenberg, eds.), pp. 759–777, Cold Spring Harbor Laboratory Press, New York.

    Google Scholar 

  • Woo, N. H., Roe, B. A., and Rich, A. (1980) Three-dimensional structure of Escherichia coli initiator tRNAf Met, Nature 286:346–351.

    Article  PubMed  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Russian Academy of Sciences, Moscow, Russia

    Alexander S. Spirin

Authors
  1. Alexander S. Spirin
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

Copyright information

© 1999 Kluwer Academic/Plenum Publishers, New York

About this chapter

Cite this chapter

Spirin, A.S. (1999). Initiation of Translation. In: Ribosomes. Cellular Organelles. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-7817-8_15

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-7817-8_15

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-0-306-46146-0

  • Online ISBN: 978-1-4615-7817-8

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation