ArticleNucleic acids research2016
Signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 41 citations in OpenAlex.
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- Structure and function of the RNA polymerase complex of Borna disease virus, a nuclear-replicating non-segmented negative-strand RNA virus.Nucleic acids research · 2026Article
- Status of advanced respiratory syncytial virus antiviral therapeutics 2025.Current opinion in virology · 2025Review
- Structural insights into the dynamic mechanism of bornavirus polymerase.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Cryo-EM structure of Nipah virus L-P polymerase complex.Nature communications · 2024Article
- Structural basis of paramyxo- and pneumovirus polymerase inhibition by non-nucleoside small-molecule antivirals.Antimicrobial agents and chemotherapy · 2024Review
- The complete pathway for co-transcriptional mRNA maturation within a large protein of a non-segmented negative-strand RNA virus.Nucleic acids research · 2024Article
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
- Structural basis for dimerization of a paramyxovirus polymerase complex.Nature communications · 2024Article
- Structural and mechanistic insights into the inhibition of respiratory syncytial virus polymerase by a non-nucleoside inhibitor.Communications biology · 2023Article
- Discontinuous L-binding motifs in the transactivation domain of the vesicular stomatitis virus P protein are required for terminalJournal of virology · 2023Article
- Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.Viruses · 2023Review
- Revisiting Viral RNA-Dependent RNA Polymerases: Insights from Recent Structural Studies.Viruses · 2022Review
- GDP polyribonucleotidyltransferase domain of vesicular stomatitis virus polymerase regulates leader-promoter escape and polyadenylation-coupled termination during stop-start transcription.PLoS pathogens · 2022Article
- Enzymatic Assays to Explore Viral mRNA Capping Machinery.Chembiochem : a European journal of chemical biology · 2021Review
- First insights into the structural features of Ebola virus methyltransferase activities.Nucleic acids research · 2021Article
- Structures of theJournal of virology · 2020Review
- Structure of a rabies virus polymerase complex from electron cryo-microscopy.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase; block V) domain in RNA polymerase L proteins of non-segmented negative strand (NNS) RNA viruses (e.g. rabies, measles, Ebola) contains five collinear sequence elements, Rx(3)Wx(3-8)ΦxGxζx(P/A) (motif A; Φ, hydrophobic; ζ, hydrophilic), (Y/W)ΦGSxT (motif B), W (motif C), HR (motif D) and ζxxΦx(F/Y)QxxΦ (motif E). We performed site-directed mutagenesis of the L protein of vesicular stomatitis virus (VSV, a prototypic NNS RNA virus) to examine participation of these motifs in mRNA capping. Similar to the catalytic residues in motif D, G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E were found to be essential or important for the PRNTase activity in the step of the covalent L-pRNA intermediate formation, but not for the GTPase activity that generates GDP (pRNA acceptor). Cap defective mutations in these residues induced termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolished virus gene expression in host cells. These results suggest that the conserved motifs constitute the active site of the PRNTase domain and the L-pRNA intermediate formation followed by the cap formation is essential for successful synthesis of full-length mRNAs.
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