title: The L protein of vesicular stomatitis virus modulates the response of the polyadenylic acid polymerase to S-adenosylhomocysteine.
abstract: 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.
authors.affiliation: Department of Microbiology and Immunology, University of South Carolina School of Medicine, Columbia 29208.
authors.forename: D M
authors.initials: DM
authors.lastname: Hunt
authors.forename: R
authors.initials: R
authors.lastname: Mehta
authors.forename: K L
authors.initials: KL
authors.lastname: Hutchinson
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism; D002213:Capsid / Q000302:isolation & purification / Q000378:metabolism; D006710:Homocysteine / Q000031:analogs & derivatives*; D009154:Mutation; D009713:Nucleotidyltransferases / Q000096:biosynthesis*; D011062:Polynucleotide Adenylyltransferase / Q000096:biosynthesis*; D012324:RNA-Dependent RNA Polymerase; D012435:S-Adenosylhomocysteine / Q000494:pharmacology*; D013045:Species Specificity; D014542:Uridine Monophosphate / Q000378:metabolism; D014721:Vesicular stomatitis Indiana virus / Q000235:genetics / Q000378:metabolism*; D014758:Viral Core Proteins / Q000302:isolation & purification / Q000378:metabolism; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins / Q000302:isolation & purification / Q000502:physiology*
chemical_list: D014758:Viral Core Proteins; D017361:Viral Nonstructural Proteins; D014764:Viral Proteins; D006710:Homocysteine; D000249:Adenosine Monophosphate; D012435:S-Adenosylhomocysteine; D014542:Uridine Monophosphate; D009713:Nucleotidyltransferases; D011062:Polynucleotide Adenylyltransferase; C040530:L protein, vesicular stomatitis virus; D012324:RNA-Dependent RNA Polymerase