Possible in vitro repair of viral RNA by ligase-like enzyme(s) in poliovirus-infected cells.
A soluble polymerase-template complex prepared from poliovirus-infected cells was found to incorporate radioactive UTP into trichloroacetic acid-insoluble RNA linearly for 8 h in the presence of ATP and Mg2+. Radioactive CTP or GTP was not incorporated under identical conditions. Nearest-neighbor analysis of the in vitro product demonstrated that ATP was added to the viral RNA in the form of polyadenylic acid; UTP was added internally to the 3'-OH group of all four nucelotides. The data can best be explained by the addition of the UTP to the 3'-OH groups of single-stranded breaks in the double-stranded viral RNA and ligation to the adjacent 5'-phosphate groups. The enzymatic activity was also found in encephalomyocarditis virus- and rhinovirus type 1A-infected cells but not in uninfected cells.
D000255:Adenosine Triphosphate / Q000378:metabolism; D012321:DNA-Directed RNA Polymerases / Q000378:metabolism; D004686:Encephalomyocarditis virus / Q000201:enzymology; D006367:HeLa Cells; D008025:Ligases / Q000378:metabolism*; D008274:Magnesium / Q000378:metabolism; D017955:Poliovirus / Q000201:enzymology / Q000378:metabolism*; D012367:RNA, Viral / Q000096:biosynthesis*; D012229:Rhinovirus / Q000201:enzymology; D013698:Templates, Genetic; D014500:Uracil Nucleotides / Q000378:metabolism
D012367:RNA, Viral; D014500:Uracil Nucleotides; D000255:Adenosine Triphosphate; D012321:DNA-Directed RNA Polymerases; D008025:Ligases; D008274:Magnesium