ArticleProceedings of the National Academy of Sciences of the United States of America2024
Cryo-EM structure and functional landscape of an RNA polymerase ribozyme.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
13 citing papers in PubMed.
- Molecular insights into dynamic RNA quaternary assemblies.RNA biology · 2026Review
- Exonuclease Ribozyme Encoded in a Circular Genome: On the Initiation of the RNA World.Life (Basel, Switzerland) · 2026Article
- Structure and catalytic activity of the SAM-utilizing ribozyme SAMURI.Nature chemical biology · 2026Article
- A universal Fab targeting a conserved U1A-RNA epitope for RNA structure determination by cryo-EM.Nucleic acids research · 2026Article
- A small polymerase ribozyme that can synthesize itself and its complementary strand.Science (New York, N.Y.) · 2026Article
- Brave new RNA world(s): from prebiotic chemistry to gene regulation and RNA technology.Frontiers in genetics · 2026Review
- The power of triplets.Nature reviews. Chemistry · 2025Article
- Trinucleotide substrates under pH-freeze-thaw cycles enable open-ended exponential RNA replication by a polymerase ribozyme.Nature chemistry · 2025Article
- Roles of dimeric intermediates in RNA-catalyzed rolling circle synthesis.Nucleic acids research · 2025Article
- RNA sample optimization for cryo-EM analysis.Nature protocols · 2025Review
- gRNAde: Geometric Deep Learning for 3D RNA inverse design.bioRxiv : the preprint server for biology · 2025Article
- Biomathematical enzyme kinetics model of prebiotic autocatalytic RNA networks: degenerating parasite-specific hyperparasite catalysts confer parasite resistance and herald the birth of molecular immunity.PLoS computational biology · 2025Article
- Architecture of an RNA polymerase ribozyme illuminates the RNA World.Trends in genetics : TIG · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
Abstract
The emergence of an RNA replicase capable of self-replication is considered an important stage in the origin of life. RNA polymerase ribozymes (PR) - including a variant that uses trinucleotide triphosphates (triplets) as substrates - have been created by in vitro evolution and are the closest functional analogues of the replicase, but the structural basis for their function is poorly understood. Here we use single-particle cryogenic electron microscopy (cryo-EM) and high-throughput mutation analysis to obtain the structure of a triplet polymerase ribozyme (TPR) apoenzyme and map its functional landscape. The cryo-EM structure at 5-Å resolution reveals the TPR as an RNA heterodimer comprising a catalytic subunit and a noncatalytic, auxiliary subunit, resembling the shape of a left hand with thumb and fingers at a 70° angle. The two subunits are connected by two distinct kissing-loop (KL) interactions that are essential for polymerase function. Our combined structural and functional data suggest a model for templated RNA synthesis by the TPR holoenzyme, whereby heterodimer formation and KL interactions preorganize the TPR for optimal primer-template duplex binding, triplet substrate discrimination, and templated RNA synthesis. These results provide a better understanding of TPR structure and function and should aid the engineering of more efficient PRs.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.