Purified vesicular stomatitis virus contains an enzyme activity that synthesizes cytidylyl (5'-3') guanosine 5'-triphosphate in vitro.

Abstract

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.

• Authors: P K Chanda, A K Banerjee
• Journal: The Journal of biological chemistry (J Biol Chem) Vol. 256 Issue 22 Pg. 11393-6 (Nov 25 1981) ISSN: 0021-9258 [Print] United States
• PMID: 6271745 (Publication Type: Journal Article)

Chemical References

• Oligonucleotides
• Cytidine Triphosphate
• guanosine triphosphate cytidine monophosphate
• Guanosine Triphosphate

Topics

• Animals
• Cell Line
• Cricetinae
• Cytidine Triphosphate (metabolism)
• Guanosine Triphosphate (metabolism)
• Kidney
• Kinetics
• Oligonucleotides (biosynthesis)
• Vesicular stomatitis Indiana virus (enzymology)