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 Letters

Agol, V.I.¹  Ugarova, T.Yu.²  Siyanova, E.Yu.²  Baratova, L.A.²  Svitkin, Yu.V.¹  Kazachkov, Yu.A.¹ 

[1] Institute of Poliomyelitis and Viral Encephalitides, the USSR Academy of Medical Sciences, Moscow Region 142782, USSR;A.N. Belozersky Laboratory of Molecular Biology and Bioorganic Chemistry, Moscow State University, W-234, Moscow 119899 USSR

关键词: Picornavirus;    Cell-free protein synthesis;    Translation initiation;    Polyprotein processing;    Radiochemical sequence analysis;   

DOI  :  10.1016/0014-5793(84)81340-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown