Sequence determination of the capsid protein gene and flanking regions of tobacco etch virus: evidence for synthesis and processing of a polyprotein in potyvirus genome expression

• Published in: Proceedings of the National Academy of Sciences - PNAS 1985-06, Vol.82 (12), p.3969-3972
• Main Authors: Allison, R.F, Sorenson, J.C, Kelly, M.E, Armstrong, F.B, Dougherty, W.G
• Format: Article
• Language: English
• Subjects: Amino acids; Biological and medical sciences; Biological Sciences: Biochemistry; Capsid proteins; Complementary DNA; Fundamental and applied biological sciences. Psychology; Generally accepted auditing standards; GENOMAS; GENOME; GENOMES; Microbiology; Molecular weight; NUCLEOTIDE; Nucleotide sequences; NUCLEOTIDES; NUCLEOTIDOS; Open reading frames; PLANT VIRUSES; Replicative cycle, interference, host-virus relations, pathogenicity, miscellaneous strains; RNA; tobacco etch virus; Virology; VIRUS DE LAS PLANTAS; VIRUS DES VEGETAUX
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.82.12.3969

The nucleotide sequence of the 3′-terminal portion of the tobacco etch virus (TEV) genome was determined. The 2324-nucleotide sequence represented approximately one-fourth of the TEV genome and included the capsid protein gene and flanking regions. An open reading frame of 2135 nucleotides and an untranslated region of 189 nucleotides adjacent to a polyadenylate tract were identified. The sequence began within an open reading frame, indicating that the initiation codon was upstream of the available sequence data. The sequence of the 20 NH2-terminal amino acids of the TEV capsid protein was established chemically. An identical amino acid sequence, predicted from the nucleotide sequence, was located, commencing at amino acid -263. These data indicated that maturation of the capsid protein required a post-translational cleavage of a larger protein precursor, with a probable cleavage site between the amino acids glutamine and glycine.