The L Protein of Vesicular Stomatitis Virus Modulates the Response of the Polyadenylic Acid Polymerase to S-Adenosylhomocysteine

• Published in: Journal of general virology 1988-10, Vol.69 (10), p.2555-2561
• Main Authors: Hunt, D. Margaret, Mehta, Roshni, Hutchinson, Karen L
• Format: Article
• Language: English
• Subjects: Adenosine Monophosphate - metabolism; Biological and medical sciences; Capsid - isolation & purification; Capsid - metabolism; Fundamental and applied biological sciences. Psychology; Genetics; Homocysteine - analogs & derivatives; Microbiology; Mutation; Nucleotidyltransferases - biosynthesis; Polynucleotide Adenylyltransferase - biosynthesis; RNA Replicase; S-Adenosylhomocysteine - pharmacology; Species Specificity; Uridine Monophosphate - metabolism; Vesicular stomatitis Indiana virus - genetics; Vesicular stomatitis Indiana virus - metabolism; vesicular stomatitis virus; Viral Core Proteins - isolation & purification; Viral Core Proteins - metabolism; Viral Nonstructural Proteins; Viral Proteins - isolation & purification; Viral Proteins - physiology; Virology
• ISSN: 0022-1317; 1465-2099
• DOI: 10.1099/0022-1317-69-10-2555

1 Department of Microbiology and Immunology, University of South Carolina School of Medicine, Columbia, South Carolina 29208 and 2 Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, U.S.A. Ts G16(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 ts G16(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 ts G16(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 ts G16(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. Keywords: VSV, polyadenylation, L protein Present address: Plant Hormone Laboratory, USDA, ARS, Beltsville Agriculture Research Center, Beltsville, Maryland 20705, U.S.A. Received 1 March 1988; accepted 22 June 1988.