Characterization of a 70S polyuridylic acid polymerase isolated from foot-and-mouth disease virus-infected cells.
A polyuridylic acid polymerase complex isolated from foot-and-mouth disease virus-infected cells sedimented at 70S in a sucrose gradient and appeared in the exclusion volume of an agarose column whose molecular weight cutoff was 5 x 10(6). Phenol extraction of the complex yielded a heterogeneous band of virus-specific RNA and an apparently host cell-derived 4.5 to 5S RNA, both of which are essentially single stranded. Neither RNA served as a template in the cell-free enzyme reaction. Polyacrylamide gel analysis revealed five polypeptides with molecular weights of 50,000, 56,000, 60,000, 70,000, and 74,000 and with molar ratios of 1:2:2:1:1, respectively. Autoradiography showed P56 to be the only major virus-induced polypeptide; the other proteins are apparently of host cell origin. Electron microscopic examination suggested a cartwheel shape for the polymerase complex which was seen to dissociate as polyadenylic acid was added. Antibody previously shown to inhibit enzyme activity aggregated the 70S units.
D000818:Animals; D005537:Aphthovirus / Q000201:enzymology*; D002460:Cell Line; D002499:Centrifugation, Density Gradient; D006224:Cricetinae; D008854:Microscopy, Electron; D008968:Molecular Conformation; D008970:Molecular Weight; D009713:Nucleotidyltransferases / Q000032:analysis*; D011072:Poly U / Q000032:analysis; D011506:Proteins / Q000032:analysis; D012367:RNA, Viral / Q000032:analysis; D014764:Viral Proteins / Q000032:analysis
D011506:Proteins; D012367:RNA, Viral; D014764:Viral Proteins; D011072:Poly U; D009713:Nucleotidyltransferases; C022428:poly U polymerase