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. 1988 Sep;7(9):2869–2874. doi: 10.1002/j.1460-2075.1988.tb03143.x

Scanning independent ribosomal initiation of the Sendai virus X protein.

J Curran 1, D Kolakofsky 1
PMCID: PMC457080  PMID: 2846286

Abstract

Both peptide antisera and monoclonal antibodies detect a 10-kd protein (X) in Sendai virus infected cells, which represents approximately the last 95 residues of the 568-amino-acid-long P protein. The X protein does not appear to be derived from a precursor P in vivo, and in in vitro X can be made under conditions in which P synthesis has been arrested by hybridized DNA fragments or specific cleavage of the mRNA. X initiation is nevertheless cap dependent. Ribosomes which initiate X appear to pass directly from the cap to the initiation codon.

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Selected References

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  1. Abramson R. D., Dever T. E., Lawson T. G., Ray B. K., Thach R. E., Merrick W. C. The ATP-dependent interaction of eukaryotic initiation factors with mRNA. J Biol Chem. 1987 Mar 15;262(8):3826–3832. [PubMed] [Google Scholar]
  2. Abramson R. D., Dever T. E., Merrick W. C. Biochemical evidence supporting a mechanism for cap-independent and internal initiation of eukaryotic mRNA. J Biol Chem. 1988 May 5;263(13):6016–6019. [PubMed] [Google Scholar]
  3. Banerjee A. K. 5'-terminal cap structure in eucaryotic messenger ribonucleic acids. Microbiol Rev. 1980 Jun;44(2):175–205. doi: 10.1128/mr.44.2.175-205.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Collins P. L., Wertz G. W., Ball L. A., Hightower L. E. Coding assignments of the five smaller mRNAs of Newcastle disease virus. J Virol. 1982 Sep;43(3):1024–1031. doi: 10.1128/jvi.43.3.1024-1031.1982. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Curran J. A., Kolakofsky D. Identification of an additional Sendai virus non-structural protein encoded by the P/C mRNA. J Gen Virol. 1987 Sep;68(Pt 9):2515–2519. doi: 10.1099/0022-1317-68-9-2515. [DOI] [PubMed] [Google Scholar]
  6. Curran J., Kolakofsky D. Ribosomal initiation from an ACG codon in the Sendai virus P/C mRNA. EMBO J. 1988 Jan;7(1):245–251. doi: 10.1002/j.1460-2075.1988.tb02806.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Darlix J. L., Zuker M., Spahr P. F. Structure-function relationship of Rous sarcoma virus leader RNA. Nucleic Acids Res. 1982 Sep 11;10(17):5183–5196. doi: 10.1093/nar/10.17.5183. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Gill D. S., Banerjee A. K. Vesicular stomatitis virus NS proteins: structural similarity without extensive sequence homology. J Virol. 1985 Jul;55(1):60–66. doi: 10.1128/jvi.55.1.60-66.1985. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Gill D. S., Chattopadhyay D., Banerjee A. K. Identification of a domain within the phosphoprotein of vesicular stomatitis virus that is essential for transcription in vitro. Proc Natl Acad Sci U S A. 1986 Dec;83(23):8873–8877. doi: 10.1073/pnas.83.23.8873. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Giorgi C., Blumberg B. M., Kolakofsky D. Sendai virus contains overlapping genes expressed from a single mRNA. Cell. 1983 Dec;35(3 Pt 2):829–836. doi: 10.1016/0092-8674(83)90115-0. [DOI] [PubMed] [Google Scholar]
  11. 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]
  12. Hamaguchi M., Yoshida T., Nishikawa K., Naruse H., Nagai Y. Transcriptive complex of Newcastle disease virus. I. Both L and P proteins are required to constitute an active complex. Virology. 1983 Jul 15;128(1):105–117. doi: 10.1016/0042-6822(83)90322-7. [DOI] [PubMed] [Google Scholar]
  13. Herman R. C. Internal initiation of translation on the vesicular stomatitis virus phosphoprotein mRNA yields a second protein. J Virol. 1986 Jun;58(3):797–804. doi: 10.1128/jvi.58.3.797-804.1986. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Herrler G., Compans R. W. Synthesis of mumps virus polypeptides in infected Vero cells. Virology. 1982 Jun;119(2):430–438. doi: 10.1016/0042-6822(82)90102-7. [DOI] [PubMed] [Google Scholar]
  15. Huang W. M., Ao S. Z., Casjens S., Orlandi R., Zeikus R., Weiss R., Winge D., Fang M. A persistent untranslated sequence within bacteriophage T4 DNA topoisomerase gene 60. Science. 1988 Feb 26;239(4843):1005–1012. doi: 10.1126/science.2830666. [DOI] [PubMed] [Google Scholar]
  16. Konarska M. M., Padgett R. A., Sharp P. A. Recognition of cap structure in splicing in vitro of mRNA precursors. Cell. 1984 Oct;38(3):731–736. doi: 10.1016/0092-8674(84)90268-x. [DOI] [PubMed] [Google Scholar]
  17. Kozak M. Effects of intercistronic length on the efficiency of reinitiation by eucaryotic ribosomes. Mol Cell Biol. 1987 Oct;7(10):3438–3445. doi: 10.1128/mcb.7.10.3438. [DOI] [PMC free article] [PubMed] [Google Scholar]
  18. Kozak M. How do eucaryotic ribosomes select initiation regions in messenger RNA? Cell. 1978 Dec;15(4):1109–1123. doi: 10.1016/0092-8674(78)90039-9. [DOI] [PubMed] [Google Scholar]
  19. Kozak M. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell. 1986 Jan 31;44(2):283–292. doi: 10.1016/0092-8674(86)90762-2. [DOI] [PubMed] [Google Scholar]
  20. Lax S., Fritz W., Browning K., Ravel J. Isolation and characterization of factors from wheat germ that exhibit eukaryotic initiation factor 4B activity and overcome 7-methylguanosine 5'-triphosphate inhibition of polypeptide synthesis. Proc Natl Acad Sci U S A. 1985 Jan;82(2):330–333. doi: 10.1073/pnas.82.2.330. [DOI] [PMC free article] [PubMed] [Google Scholar]
  21. Lee K. A., Sonenberg N. Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus. Proc Natl Acad Sci U S A. 1982 Jun;79(11):3447–3451. doi: 10.1073/pnas.79.11.3447. [DOI] [PMC free article] [PubMed] [Google Scholar]
  22. Marth J. D., Overell R. W., Meier K. E., Krebs E. G., Perlmutter R. M. Translational activation of the lck proto-oncogene. Nature. 1988 Mar 10;332(6160):171–173. doi: 10.1038/332171a0. [DOI] [PubMed] [Google Scholar]
  23. Minshull J., Hunt T. The use of single-stranded DNA and RNase H to promote quantitative 'hybrid arrest of translation' of mRNA/DNA hybrids in reticulocyte lysate cell-free translations. Nucleic Acids Res. 1986 Aug 26;14(16):6433–6451. doi: 10.1093/nar/14.16.6433. [DOI] [PMC free article] [PubMed] [Google Scholar]
  24. Mueller P. P., Harashima S., Hinnebusch A. G. A segment of GCN4 mRNA containing the upstream AUG codons confers translational control upon a heterologous yeast transcript. Proc Natl Acad Sci U S A. 1987 May;84(9):2863–2867. doi: 10.1073/pnas.84.9.2863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  25. Mueller P. P., Hinnebusch A. G. Multiple upstream AUG codons mediate translational control of GCN4. Cell. 1986 Apr 25;45(2):201–207. doi: 10.1016/0092-8674(86)90384-3. [DOI] [PubMed] [Google Scholar]
  26. Patwardhan S., Gupta K. C. Translation initiation potential of the 5' proximal AUGs of the polycistronic P/C mRNA of Sendai virus. A multipurpose vector for site-specific mutagenesis. J Biol Chem. 1988 Apr 5;263(10):4907–4913. [PubMed] [Google Scholar]
  27. Peluso R. W., Lamb R. A., Choppin P. W. Polypeptide synthesis in simian virus 5-infected cells. J Virol. 1977 Jul;23(1):177–187. doi: 10.1128/jvi.23.1.177-187.1977. [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Petersen R. B., Hensel C. H., Hackett P. B. Identification of a ribosome-binding site for a leader peptide encoded by Rous sarcoma virus RNA. J Virol. 1984 Sep;51(3):722–729. doi: 10.1128/jvi.51.3.722-729.1984. [DOI] [PMC free article] [PubMed] [Google Scholar]
  29. Ray B. K., Brendler T. G., Adya S., Daniels-McQueen S., Miller J. K., Hershey J. W., Grifo J. A., Merrick W. C., Thach R. E. Role of mRNA competition in regulating translation: further characterization of mRNA discriminatory initiation factors. Proc Natl Acad Sci U S A. 1983 Feb;80(3):663–667. doi: 10.1073/pnas.80.3.663. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Rima B. K., Roberts M. W., McAdam W. D., Martin S. J. Polypeptide synthesis i mumps virus-infected cells. J Gen Virol. 1980 Feb;46(2):501–505. doi: 10.1099/0022-1317-46-2-501. [DOI] [PubMed] [Google Scholar]
  31. Sonenberg N. Regulation of translation by poliovirus. Adv Virus Res. 1987;33:175–204. doi: 10.1016/s0065-3527(08)60318-8. [DOI] [PubMed] [Google Scholar]
  32. Spriggs M. K., Collins P. L. Sequence analysis of the P and C protein genes of human parainfluenza virus type 3: patterns of amino acid sequence homology among paramyxovirus proteins. J Gen Virol. 1986 Dec;67(Pt 12):2705–2719. doi: 10.1099/0022-1317-67-12-2705. [DOI] [PubMed] [Google Scholar]
  33. Thomas K. R., Capecchi M. R. Introduction of homologous DNA sequences into mammalian cells induces mutations in the cognate gene. Nature. 1986 Nov 6;324(6092):34–38. doi: 10.1038/324034a0. [DOI] [PubMed] [Google Scholar]
  34. Towbin H., Staehelin T., Gordon J. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc Natl Acad Sci U S A. 1979 Sep;76(9):4350–4354. doi: 10.1073/pnas.76.9.4350. [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Tuerk C., Gauss P., Thermes C., Groebe D. R., Gayle M., Guild N., Stormo G., d'Aubenton-Carafa Y., Uhlenbeck O. C., Tinoco I., Jr CUUCGG hairpins: extraordinarily stable RNA secondary structures associated with various biochemical processes. Proc Natl Acad Sci U S A. 1988 Mar;85(5):1364–1368. doi: 10.1073/pnas.85.5.1364. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Tzamarias D., Alexandraki D., Thireos G. Multiple cis-acting elements modulate the translational efficiency of GCN4 mRNA in yeast. Proc Natl Acad Sci U S A. 1986 Jul;83(13):4849–4853. doi: 10.1073/pnas.83.13.4849. [DOI] [PMC free article] [PubMed] [Google Scholar]
  37. Vidal S., Curran J., Orvell C., Kolakofsky D. Mapping of monoclonal antibodies to the Sendai virus P protein and the location of its phosphates. J Virol. 1988 Jun;62(6):2200–2203. doi: 10.1128/jvi.62.6.2200-2203.1988. [DOI] [PMC free article] [PubMed] [Google Scholar]

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