RT Journal Article SR Electronic(1) A1 Hunt, D. Margaret A1 Mehta, Roshni A1 Hutchinson, Karen L.YR 1988 T1 The L Protein of Vesicular Stomatitis Virus Modulates the Response of the Polyadenylic Acid Polymerase to S-Adenosylhomocysteine JF Journal of General Virology, VO 69 IS 10 SP 2555 OP 2561 DO https://doi.org/10.1099/0022-1317-69-10-2555 PB Microbiology Society, SN 1465-2099, AB Summary TsG16(I) is a temperature-sensitive (ts) mutant of vesicular stomatitis virus, Indiana serotype, which overproduces polyadenylic acid [poly(A)] in an in vitro transcription system due to a mutation in the L protein. Others have reported that l-S-adenosylhomocysteine (S-Ado-Hcy) causes wild-type (wt) virus to overproduce poly(A) in vitro. The possibility that tsG16(I) constitutively expresses a property induced by S-Ado-Hcy in the case of wt virus was found not to be so since polyadenylation by the mutant was still sensitive to S-Ado-Hcy. Indeed, S-Ado-Hcy caused tsG16(I) to overproduce poly(A) in vitro to a greater extent than its parental wt virus. The increase in polyadenylation observed in response to saturating levels of S-Ado-Hcy differed for tsG16(I), for its parental wt virus and for another wt strain. To characterize which viral protein modulated the polyadenylation response to S-Ado-Hcy, purified virions were fractionated and their phenotypes in homologous and heterologous reconstitution assays were examined. The results indicated that the viral L protein modulated the response in all three stocks of virus. These data provide further evidence to suggest that the L protein of vesicular stomatitis virus plays a role in polyadenylation of the viral mRNA., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-69-10-2555