ArticleACS central science2016
Unusual Base-Pairing Interactions in Monomer-Template Complexes.
Article in ACS central science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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15 citing papers in PubMed, 32 citations in OpenAlex.
- Catalytic Metal Ion-Substrate Coordination during Nonenzymatic RNA Primer Extension.Journal of the American Chemical Society · 2024Article
- Molecular insight into how the position of an abasic site modifies DNA duplex stability and dynamics.Biophysical journal · 2024Article
- Insight into the structures of unusual base pairs in RNA complexes containing a primer/template/adenosine ligand.RSC chemical biology · 2023Article
- Structural interpretation of the effects of threo-nucleotides on nonenzymatic template-directed polymerization.Nucleic acids research · 2021Article
- A Model for the Emergence of RNA from a Prebiotically Plausible Mixture of Ribonucleotides, Arabinonucleotides, and 2'-Deoxynucleotides.Journal of the American Chemical Society · 2020Article
- Prebiotically Plausible "Patching" of RNA Backbone Cleavage through a 3'-5' Pyrophosphate Linkage.Journal of the American Chemical Society · 2019Article
- Template-Directed Catalysis of a Multistep Reaction Pathway for Nonenzymatic RNA Primer Extension.Biochemistry · 2019Article
- Electrophilic oligodeoxynucleotide synthesis using dM-Dmoc for amino protection.Beilstein journal of organic chemistry · 2019Article
- Article
- Structural Rationale for the Enhanced Catalysis of Nonenzymatic RNA Primer Extension by a Downstream Oligonucleotide.Journal of the American Chemical Society · 2018Article
- Synthesis of a Nonhydrolyzable Nucleotide Phosphoroimidazolide Analogue That Catalyzes Nonenzymatic RNA Primer Extension.Journal of the American Chemical Society · 2018Article
- A Kinetic Model of Nonenzymatic RNA Polymerization by Cytidine-5'-phosphoro-2-aminoimidazolide.Biochemistry · 2017Article
- Insight into the mechanism of nonenzymatic RNA primer extension from the structure of an RNA-GpppG complex.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Downstream Oligonucleotides Strongly Enhance the Affinity of GMP to RNA Primer-Template Complexes.Journal of the American Chemical Society · 2017Article
- Unusual Hydrogen Bonding Patterns and the Role of the Backbone in Nucleic Acid Information Transfer.ACS central science · 2016Article
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Many high-resolution crystal structures have contributed to our understanding of the reaction pathway for catalysis by DNA and RNA polymerases, but the structural basis of nonenzymatic template-directed RNA replication has not been studied in comparable detail. Here we present crystallographic studies of the binding of ribonucleotide monomers to RNA primer-template complexes, with the goal of improving our understanding of the mechanism of nonenzymatic RNA copying, and of catalysis by polymerases. To explore how activated ribonucleotides recognize and bind to RNA templates, we synthesized an unreactive phosphonate-linked pyrazole analogue of guanosine 5'-phosphoro-2-methylimidazolide (2-MeImpG), a highly activated nucleotide that has been used extensively to study nonenzymatic primer extension. We cocrystallized this analogue with structurally rigidified RNA primer-template complexes carrying single or multiple monomer binding sites, and obtained high-resolution X-ray structures of these complexes. In addition to Watson-Crick base pairing, we repeatedly observed noncanonical guanine:cytidine base pairs in our crystal structures. In most structures, the phosphate and leaving group moieties of the monomers were highly disordered, while in others the distance from O3' of the primer to the phosphorus of the incoming monomer was too great to allow for reaction. We suggest that these effects significantly influence the rate and fidelity of nonenzymatic RNA replication, and that even primitive ribozyme polymerases could enhance RNA replication by enforcing Watson-Crick base pairing between monomers and primer-template complexes, and by bringing the reactive functional groups into closer proximity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.