Poly(A) polymerase activity in reovirus.
An enzymatic activity which synthesized oligo(A) in vitro was found in highly purified reovirus. The poly(A) polymerase activity was dependent on Mn(2+) and utilized only ATP, whereas the virion-associated RNA polymerase required all four ribonucleoside triphosphates and Mg(2+). Oligo(A) synthesis was demonstrated with complete virions and infectious subviral particles derived from virus by limited chymotrypsin digestion but not with cores, a product of extensive chymotrypsin digestion of virus. The enzymatic product and the oligo(A) from purified virions were isolated by binding to oligo(dT)-cellulose columns. Most of the in vitro product was similar in size and structure to the oligo(A) from purified virions by the criteria of gel electrophoresis, DEAE-cellulose chromatography, end-group analysis, and sensitivity to RNase. The evidence suggests that oligo(A) synthesis is mediated by the poly(A) polymerase during a late step in viral morphogenesis and may result from an alternative activity of the virion-associated transcriptase.
D000255:Adenosine Triphosphate; D000468:Alkalies; D002848:Chromatography, DEAE-Cellulose; D003597:Cytosine Nucleotides; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D003851:Deoxyribonucleases; D006160:Guanosine Triphosphate; D008274:Magnesium; D008345:Manganese; D009713:Nucleotidyltransferases / Q000378:metabolism*; D009841:Oligonucleotides / Q000096:biosynthesis*; D012367:RNA, Viral / Q000096:biosynthesis; D012087:Reoviridae / Q000201:enzymology*; D012260:Ribonucleases; D013997:Time Factors; D014316:Tritium; D014500:Uracil Nucleotides
D000468:Alkalies; D003597:Cytosine Nucleotides; D009841:Oligonucleotides; D012367:RNA, Viral; D014500:Uracil Nucleotides; D014316:Tritium; D008345:Manganese; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D009713:Nucleotidyltransferases; D012321:DNA-Directed RNA Polymerases; D003851:Deoxyribonucleases; D012260:Ribonucleases; D008274:Magnesium