Cleavage of a viral polyprotein by a cellular proteolytic activity.
The 200,000-dalton polyprotein encoded by the bottom component RNA of cowpea mosaic virus was synthesized in rabbit reticulocyte lysates, and this in vitro-synthesized protein was isolated from the lysate reaction mixture by sucrose density gradient centrifugation. Incubation of the isolated polyprotein with buffer caused no change in the protein, but incubation with reticulocyte lysates or with fractionated lysate proteins resulted in cleavage of the protein into the expected cleavage products (32,000- and 170,000-dalton proteins). This finding indicated that reticulocytes contain a proteolytic activity that is needed for the primary cleavage reaction. A cleavage assay in which we used partially purified preparations showed that cleavage was an ATP-dependent reaction.
D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D004229:Dithiothreitol / Q000378:metabolism; D008970:Molecular Weight; D009029:Mosaic Viruses / Q000378:metabolism; D010447:Peptide Hydrolases / Q000378:metabolism*; D011498:Protein Precursors / Q000378:metabolism; D011817:Rabbits; D012156:Reticulocytes / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism; D014764:Viral Proteins / Q000096:biosynthesis* / Q000378:metabolism
D011498:Protein Precursors; D014452:Ubiquitins; D014764:Viral Proteins; D000255:Adenosine Triphosphate; D010447:Peptide Hydrolases; D004229:Dithiothreitol