Cell-free translation of Drosophila C virus RNA: identification of a virus protease activity involved in capsid protein synthesis and further studies on in vitro processing of cricket paralysis virus specified proteins.
Drosophila C virus RNA acted as mRNA in rabbit reticulocyte lysates and directed the synthesis of at least one capsid protein and a number of higher molecular weight proteins. Kinetic analysis by pulse-chase experiments showed that a number of high molecular weight products acted as precursors to the capsid protein(s). Various dilution experiments were performed which showed that the virus specified a protease activity essential for the correct processing of precursors to give the capsid protein(s). A similar result was obtained with Cricket paralysis virus, and mixing experiments showed that the protease activity specified by one virus could perform some of the cleavages resulting in the production of the capsid proteins of the other virus. Some of the cleavages involving the highest molecular weight precursors could not be performed by the protease activity of the other virus. We could find no evidence for intramolecular cleavage of the capsid precursors of either of the viruses.
D000818:Animals; D002213:Capsid / Q000096:biosynthesis*; D002474:Cell-Free System; D003720:Densitometry; D004331:Drosophila melanogaster; D007304:Insect Viruses; D009987:Orthoptera; D010447:Peptide Hydrolases / Q000378:metabolism*; D014176:Protein Biosynthesis; D012328:RNA Viruses / Q000235:genetics*; D012367:RNA, Viral / Q000378:metabolism*; D012190:Retroviridae / Q000235:genetics; D014764:Viral Proteins / Q000096:biosynthesis*
D012367:RNA, Viral; D014764:Viral Proteins; D010447:Peptide Hydrolases