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Query: UMLS:C0038362 (stomatitis)
 8,852 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Detergent-disrupted vesicular stomatitis virus carried out in vitro transcription at a reduced rate in the presence of deoxyguanosine triphosphate. The transcripts annealed completely to excess vesicular stomatitis virus genomic RNA and consistent of the short leader RNA and even polyadenylated messenger RNA. Incubation with RNase T1 showed that the transcripts were resistant to cleavage. Nearest-neighbor analysis demonstrated that approximately two-thirds of the guanosine residues had been replaced by deoxyguanosine. The hybrid "deoxyguanosine-RNAs" carried cap structures which contained deoxyguanosine instead of guanosine. Competition experiments using both guanosine- and deoxyguanosine triphosphates indicated that GpppA and dGpppA cap structures were synthesized in approximately equal amounts at a ratio of 20 microM guanosine triphosphate to 50 microM deoxyguanosine triphosphate. Deoxyguanosine triphosphate was accepted by the polymerases of various strains and serotypes of vesicular stomatitis virus, demonstrating that its incorporation was a common characteristic. Deoxycytidine triphosphate could also substitute for cytidine triphosphate but to a lesser degree. Deoxyadenine, deoxyuridine-, and thymidine triphosphates were not or were very poorly accepted even at concentrations of 2 MM.
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PMID:In vitro transcription of vesicular stomatitis virus. Incorporation of deoxyguanosine and deoxycytidine, and formation of deoxyguanosine caps. 627 19

The RNA synthesis machinery of non-segmented negative-sense RNA viruses comprises a ribonucleoprotein complex of the genomic RNA coated by a nucleocapsid protein (N) and associated with polymerase. Work with vesicular stomatitis virus (VSV), a prototype, supports a model of RNA synthesis whereby N is displaced from the template to allow the catalytic subunit of the polymerase, the large protein (L) to gain access to the RNA. Consistent with that model, purified L can copy synthetic RNA that contains requisite promoter sequences. Full processivity of L requires its phosphoprotein cofactor and the template-associated N. Here we demonstrate the importance of the 2' position of the RNA template and the substrate nucleotide triphosphates during initiation and elongation by L. The VSV polymerase can initiate on both DNA and RNA and can incorporate dNTPs. During elongation, the polymerase is sensitive to 2' modifications, although dNTPs can be incorporated, and mixed DNA-RNA templates can function. Modifications to the 2' position of the NTP, including 2',3'-ddCTP, arabinose-CTP, and 2'-O-methyl-CTP, inhibit polymerase, whereas 2'-amino-CTP is incorporated. The inhibitory effects of the NTPs were more pronounced on authentic N-RNA with the exception of dGTP, which is incorporated. This work underscores the sensitivity of the VSV polymerase to nucleotide modifications during initiation and elongation and highlights the importance of the 2'-hydroxyl of both template and substrate NTP. Moreover, this study demonstrates a critical role of the template-associated N protein in the architecture of the RNA-dependent RNA polymerase domain of L.
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PMID:Sensitivity of the polymerase of vesicular stomatitis virus to 2' substitutions in the template and nucleotide triphosphate during initiation and elongation. 2452 87