Purified vesicular stomatitis virus contains an enzyme activity that synthesizes cytidylyl (5'-3') guanosine 5'-triphosphate in vitro.
An enzyme activity that synthesizes cytidylyl (5'-3') guanosine 5'-triphosphate (pppGpC) in vitro has been identified in purified vesicular stomatitis virus. The activity is discernible after a lag period which is reduced in length with increasing virus concentration. The lag is eliminated by addition of pppGpC or ppGpC which are effective primers and stimulate dinucleotide synthesis linearly. The requirements of the reaction with respect to MgCl2, NaCl, and temperature are similar to those for viral mRNA synthesis in vitro. The activity, together with the viral L and NS proteins, is removed from virions by treatment with 0.8 M NaCl. The particulate fraction from infected cells that contains the transcribing subviral ribonucleoprotein particles also contains the enzyme activity. The corresponding fraction from uninfected cells does not, indicating that the activity is mediated by virus-specific proteins. Possible functions of the dinucleotide in the life cycle of the virus are discussed.
D000818:Animals; D002460:Cell Line; D006224:Cricetinae; D003570:Cytidine Triphosphate / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D007668:Kidney; D007700:Kinetics; D009841:Oligonucleotides / Q000096:biosynthesis*; D014721:Vesicular stomatitis Indiana virus / Q000201:enzymology*
D009841:Oligonucleotides; D003570:Cytidine Triphosphate; C031656:guanosine triphosphate cytidine monophosphate; D006160:Guanosine Triphosphate