ArticleNucleic acids research2019
A dual-functional priming-capping loop of rhabdoviral RNA polymerases directs terminal de novo initiation and capping intermediate formation.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 51 citations in OpenAlex.
- mRNA cap formation by the human respiratory syncytial virus large protein.Nucleic acids research · 2026Article
- 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
- Structure of the measles virus ternary polymerase complex.Nature communications · 2025Article
- Functional dissection of the C-terminal domain of rabies virus RNA polymerase L protein.Journal of virology · 2025Article
- Structural basis of Nipah virus RNA synthesis.Nature communications · 2025Article
- In Vitro Biochemical Assays to Study Respiratory Syncytial Virus Polymerase Activities.Methods in molecular biology (Clifton, N.J.) · 2025Article
- 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
- Structures of the mumps virus polymerase complex via cryo-electron microscopy.Nature communications · 2024Article
- 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
- Conserved allosteric inhibitory site on the respiratory syncytial virus and human metapneumovirus RNA-dependent RNA polymerases.Communications biology · 2023Article
- Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.Viruses · 2023Review
- Orally efficacious lead of the AVG inhibitor series targeting a dynamic interface in the respiratory syncytial virus polymerase.Science advances · 2022Article
- Distinctive features of the respiratory syncytial virus priming loop compared to other non-segmented negative strand RNA viruses.PLoS pathogens · 2022Article
- GDP polyribonucleotidyltransferase domain of vesicular stomatitis virus polymerase regulates leader-promoter escape and polyadenylation-coupled termination during stop-start transcription.PLoS pathogens · 2022Article
- Comparison of RNA synthesis initiation properties of non-segmented negative strand RNA virus polymerases.PLoS pathogens · 2021Article
- Structural insights into RNA polymerases of negative-sense RNA viruses.Nature reviews. Microbiology · 2021Review
- Consequences of Phosphorylation in a Mononegavirales Polymerase-Cofactor System.Journal of virology · 2021Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
The L proteins of rhabdoviruses, such as vesicular stomatitis virus (VSV) and rabies virus (RABV), possess an unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) domain with a loop structure protruding into an active site cavity of the RNA-dependent RNA polymerase (RdRp) domain. Here, using complementary VSV and RABV systems, we show that the loop governs RNA synthesis and capping during the dynamic stop-start transcription cycle. A conserved tryptophan residue in the loop was identified as critical for terminal de novo initiation from the genomic promoter to synthesize the leader RNA and virus replication in host cells, but not for internal de novo initiation or elongation from the gene-start sequence for mRNA synthesis or pre-mRNA capping. The co-factor P protein was found to be essential for both terminal and internal initiation. A conserved TxΨ motif adjacent the tryptophan residue in the loop was required for pre-mRNA capping in the step of the covalent enzyme-pRNA intermediate formation, but not for either terminal or internal transcription initiation. These results provide insights into the regulation of stop-start transcription by the interplay between the RdRp active site and the dual-functional priming-capping loop of the PRNTase domain in non-segmented negative strand RNA viruses.
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