Partial N-terminal amino acid sequences of polypeptides p14 and p12 of encephalomyocarditis virus are identical and correspond to the N-terminus of the viral polyprotein

FEBS Lett. 1984 May 21;170(2):339-42. doi: 10.1016/0014-5793(84)81340-x.

Abstract

Our previous data suggested that translation in an EMC virus RNA-programmed cell-free system from Krebs-2 cells is initiated predominantly at a single site and that the earliest amino acid sequences synthesized correspond to non-structural 'leader' polypeptides p14 and p12 [(1982) FEBS Lett. 141, 153-156]. Here, polypeptides p14 and p12 were labelled in vitro by tritiated amino acids, isolated and subjected to automated Edman degradation. Both polypeptides (after the loss of the N-terminal methionine) were shown to contain alanine in position 1 and glutamic acid in positions 5 and 7. These and other data demonstrate that p14 and p12 share a common N-terminal sequence. This sequence coincides precisely with the N-terminus of EMC virus polyprotein sequence deduced from the primary structure of the viral genome [(1984) Nucleic Acids Res., in press]. Thus, the single initiation site operating in our translation system corresponds to the start of the polyprotein molecule.

Publication types

  • Comparative Study

MeSH terms

  • Amino Acid Sequence
  • Base Sequence
  • Codon
  • Encephalomyocarditis virus / genetics*
  • Genes, Viral*
  • Peptide Chain Initiation, Translational*
  • Peptide Fragments
  • Protein Biosynthesis
  • RNA, Viral / metabolism*
  • Viral Proteins / genetics*

Substances

  • Codon
  • Peptide Fragments
  • RNA, Viral
  • Viral Proteins