PubMed Health⌕ Search

Biomedical subjects

Kazachkov YuA

Publications and source records attributed to Kazachkov YuA.

5 recordsLinked to original sources
PubMed1984

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.

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.

Amino Acid Sequence↗
PubMed1983

The position of polypeptide G on the encephalomyocarditis virus polyprotein cleavage map.

The two-dimensional mapping of tryptic peptides of encephalomyocarditis virus-specific proteins has demonstrated that the amino acid sequence of non-structural polypeptide G constitutes a portion of the molecule of a precursor of capsid proteins, polypeptide A. The results of pulse-chase in vitro translation experiments strongly suggest that polypeptide G corresponds to a C-terminal moiety of polypeptide A. Variations in the polyprotein cleavage maps of different picornaviruses are briefly discussed.

Capsid↗