Characterization of the large picornaviral polypeptides produced in the presence of zinc ion.
Zinc ion inhibits the posttranslational cleavages of human rhinovirus-1A, encephalomyocarditis virus, and poliovirus polypeptides. Each virus displayed a different susceptibility to zinc. However, in each case the cleavages of the capsid precursor and the cleavages analogous to the C --> D --> E conversion in encephalomyocarditis virus were most sensitive to zinc. Higher concentrations of zinc resulted in the buildup of even larger precursor polypeptides of a size between 106,000 and 214,000 daltons. The sizes of these polypeptides and the relative position of their gene loci on the viral RNA were determined. These data were used to place these polypeptides in the over-all scheme of viral protein processing.
D004591:Electrophoresis, Polyacrylamide Gel; D004686:Encephalomyocarditis virus / Q000032:analysis / Q000378:metabolism*; D008970:Molecular Weight; D010452:Peptide Biosynthesis; D010455:Peptides / Q000032:analysis / Q000378:metabolism; D017955:Poliovirus / Q000032:analysis / Q000378:metabolism*; D011498:Protein Precursors / Q000032:analysis / Q000096:biosynthesis / Q000378:metabolism; D012229:Rhinovirus / Q000032:analysis / Q000378:metabolism*; D014764:Viral Proteins / Q000032:analysis / Q000096:biosynthesis* / Q000378:metabolism; D015032:Zinc / Q000494:pharmacology*
D010455:Peptides; D011498:Protein Precursors; D014764:Viral Proteins; D015032:Zinc