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

Roshni Mehta^2,

¹ Department of Microbiology and Immunology, University of South Carolina School of Medicine, Columbia, South Carolina 29208
and² Department of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, U.S.A.

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.

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.

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