ArticleThe Journal of biological chemistry2007
Structure-function relationships of the viral RNA-dependent RNA polymerase: fidelity, replication speed, and initiation mechanism determined by a residue in the ribose-binding pocket.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
36 citing papers in PubMed, 54 citations in OpenAlex.
- Identification of fidelity-determined residues of Porcine reproductive and respiratory syndrome virus through structural alignment.Virulence · 2026Article
- Replication of the coronavirus genome: A paradox among positive-strand RNA viruses.The Journal of biological chemistry · 2022Review
- RNA Viral Vectors for Accelerating Plant Synthetic Biology.Frontiers in plant science · 2021Article
- Rational Control of Poliovirus RNA-Dependent RNA Polymerase Fidelity by Modulating Motif-D Loop Conformational Dynamics.Biochemistry · 2019Article
- Attenuation of Foot-and-Mouth Disease Virus by Engineered Viral Polymerase Fidelity.Journal of virology · 2017Article
- The not-so-infinite malleability of RNA viruses: Viral and cellular determinants of RNA virus mutation rates.PLoS pathogens · 2017Review
- Triphosphate Reorientation of the Incoming Nucleotide as a Fidelity Checkpoint in Viral RNA-dependent RNA Polymerases.The Journal of biological chemistry · 2017Article
- Mechanisms of viral mutation.Cellular and molecular life sciences : CMLS · 2016Review
- Homology-Based Identification of a Mutation in the Coronavirus RNA-Dependent RNA Polymerase That Confers Resistance to Multiple Mutagens.Journal of virology · 2016Article
- Fidelity Variants and RNA Quasispecies.Current topics in microbiology and immunology · 2016Review
- RNA-Dependent RNA Polymerases of Picornaviruses: From the Structure to Regulatory Mechanisms.Viruses · 2015Review
- Insights into RNA synthesis, capping, and proofreading mechanisms of SARS-coronavirus.Virus research · 2014Review
- RNA virus population diversity, an optimum for maximal fitness and virulence.The Journal of biological chemistry · 2014Article
- Changes in protein domains outside the catalytic site of the bacteriophage Qβ replicase reduce the mutagenic effect of 5-azacytidine.Journal of virology · 2014Article
- Alphavirus mutator variants present host-specific defects and attenuation in mammalian and insect models.PLoS pathogens · 2014Article
- Variation in RNA virus mutation rates across host cells.PLoS pathogens · 2014Article
- Article
- Vaccine-derived mutation in motif D of poliovirus RNA-dependent RNA polymerase lowers nucleotide incorporation fidelity.The Journal of biological chemistry · 2013Article
- Repeated exposure to 5D9, an inhibitor of 3D polymerase, effectively limits the replication of foot-and-mouth disease virus in host cells.Antiviral research · 2013Article
- Highly similar structural frames link the template tunnel and NTP entry tunnel to the exterior surface in RNA-dependent RNA polymerases.Nucleic acids research · 2013Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Studies of the RNA-dependent RNA polymerase (RdRp) from poliovirus (PV), 3Dpol, have shown that Asn-297 permits this enzyme to distinguish ribose from 2'-deoxyribose. All animal RNA viruses have Asn at the structurally homologous position of their polymerases, suggesting a conserved function for this residue. However, all prokaryotic RNA viruses have Glu at this position. In the presence of Mg2+, the apparent affinity of Glu-297 3Dpol for 2'-deoxyribonucleotides was decreased by 6-fold relative to wild type without a substantial difference in the fidelity of 2'-dNMP incorporation. The fidelity of ribonucleotide misincorporation for Glu-297 3Dpol was reduced by 14-fold relative to wild type. A 4- to 11-fold reduction in the rate of ribonucleotide incorporation was observed. Glu-297 PV was unable to grow in HeLa cells due to a replication defect equivalent to that observed for a mutant PV encoding an inactive polymerase. Evaluation of the protein-(VPg)-primed initiation reaction showed that only half of the Glu-297 3Dpol initiation complexes were capable of producing VPg-pUpU product and that the overall yield of uridylylated VPg products was reduced by 20-fold relative to wild-type enzyme, a circumstance attributable to a reduced affinity for UTP. These studies identify the first RdRp derivative with a mutator phenotype and provide a mechanistic basis for the elevated mutation frequency of RNA phage relative to animal RNA viruses observed in culture. Although protein-primed initiation and RNA-primed elongation complexes employ the same polymerase active site, the functional differences reported here imply significant structural differences between these complexes.
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