Efficient translation of the coat protein cistron of tobacco mosaic virus in a cell-free system from Escherichia coli - PubMed (original) (raw)
Efficient translation of the coat protein cistron of tobacco mosaic virus in a cell-free system from Escherichia coli
J F Glover et al. Eur J Biochem. 1982.
Free article
Abstract
Translation of tobacco mosaic virus (TMV) RNA in a cell-free system derived from Escherichia coli (MRE 600) reveals several discrete polypeptides in the Mr range of 10,000-50,000. The major product is a polypeptide of Mr 17,500 which comigrates with authentic TMV coat protein on sodium dodecyl sulphate/polyacrylamide gel electrophoresis. Structural investigations by peptide-mapping techniques and differential radiolabelling confirm that the major product is TMV coat protein with an N-terminal methionine. The major polypeptide product can be assembled in vitro into virus-like ribonucleoprotein particles. The structural and evolutionary implications of this observation, and the values of TMV in elucidating eukaryotic mRNA interactions with the prokaryotic protein-synthesizing machinery, are discussed.
Similar articles
- The cell-free synthesis and assembly of viral specific polypeptides into TMV particles.
Roberts BE, Paterson BM, Sperling R. Roberts BE, et al. Virology. 1974 May;59(1):307-13. doi: 10.1016/0042-6822(74)90227-x. Virology. 1974. PMID: 4826210 No abstract available. - [Analysis of polypeptides of virus-specific informosomes induced by tobacco mosaic virus and potato virus X].
Dorokhov IuL, Miroshnichenko NA, Aleksandrova NM, Atabekov IG. Dorokhov IuL, et al. Mol Biol (Mosk). 1984 Jul-Aug;18(4):1001-10. Mol Biol (Mosk). 1984. PMID: 6504024 Russian. - Coat-protein-mediated resistance to tobacco mosaic virus: discovery mechanisms and exploitation.
Beachy RN. Beachy RN. Philos Trans R Soc Lond B Biol Sci. 1999 Mar 29;354(1383):659-64. doi: 10.1098/rstb.1999.0418. Philos Trans R Soc Lond B Biol Sci. 1999. PMID: 10212946 Free PMC article. Review. - Historical overview of research on the tobacco mosaic virus genome: genome organization, infectivity and gene manipulation.
Okada Y. Okada Y. Philos Trans R Soc Lond B Biol Sci. 1999 Mar 29;354(1383):569-82. doi: 10.1098/rstb.1999.0408. Philos Trans R Soc Lond B Biol Sci. 1999. PMID: 10212936 Free PMC article. Review.
Cited by
- Internal ribosome entry site from crucifer tobamovirus promotes initiation of translation in Escherichia coli.
Komarova TV, Skulachev MV, Ivanov PA, Klyushin AG, Dorokhov YL, Atabekov JG. Komarova TV, et al. Dokl Biochem Biophys. 2003 Mar-Apr;389:118-21. doi: 10.1023/a:1023644408333. Dokl Biochem Biophys. 2003. PMID: 12856419 No abstract available. - Comparison of initiation of protein synthesis in procaryotes, eucaryotes, and organelles.
Kozak M. Kozak M. Microbiol Rev. 1983 Mar;47(1):1-45. doi: 10.1128/mr.47.1.1-45.1983. Microbiol Rev. 1983. PMID: 6343825 Free PMC article. Review. No abstract available. - The 5'-leader sequence of tobacco mosaic virus RNA enhances the expression of foreign gene transcripts in vitro and in vivo.
Gallie DR, Sleat DE, Watts JW, Turner PC, Wilson TM. Gallie DR, et al. Nucleic Acids Res. 1987 Apr 24;15(8):3257-73. doi: 10.1093/nar/15.8.3257. Nucleic Acids Res. 1987. PMID: 3575095 Free PMC article. - Expression of tobacco mosaic virus coat protein and assembly of pseudovirus particles in Escherichia coli.
Hwang DJ, Roberts IM, Wilson TM. Hwang DJ, et al. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):9067-71. doi: 10.1073/pnas.91.19.9067. Proc Natl Acad Sci U S A. 1994. PMID: 8090770 Free PMC article. - Tobacco mosaic virus RNA enters chloroplasts in vivo.
Schoelz JE, Zaitlin M. Schoelz JE, et al. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4496-500. doi: 10.1073/pnas.86.12.4496. Proc Natl Acad Sci U S A. 1989. PMID: 16578844 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources
Medical