ArticleNature communications2023
Recognition and cleavage mechanism of intron-containing pre-tRNA by human TSEN endonuclease complex.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
What it found
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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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Who cites it
11 citing papers in PubMed, 12 citations in OpenAlex.
- DNTTIP2 coordinates RNA exosome activities to ensure fidelity of human ribosome assembly.Nature communications · 2026Article
- The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026Review
- Generating cerebellar organoids from pluripotent stem cells.Disease models & mechanisms · 2026Review
- Structural basis of substrate diversity and functional evolution of archaeal RNA-splicing endonucleases.Nucleic acids research · 2025Article
- Specific tRNAs promote mRNA decay by recruiting the CCR4-NOT complex to translating ribosomes.Science (New York, N.Y.) · 2024Article
- Metabolic regulation of cytoskeleton functions by HDAC6-catalyzed α-tubulin lactylation.Nature communications · 2024Article
- The molecular basis of tRNA selectivity by human pseudouridine synthase 3.Molecular cell · 2024Article
- Human organoid model of pontocerebellar hypoplasia 2a recapitulates brain region-specific size differences.Disease models & mechanisms · 2024Article
- The making and breaking of tRNAs by ribonucleases.Trends in genetics : TIG · 2024Review
- Recognition of the tRNA structure: Everything everywhere but not all at once.Cell chemical biology · 2024Review
- Metabolism Meets Translation: Dietary and Metabolic Influences on tRNA Modifications and Codon Biased Translation.Wiley interdisciplinary reviews. RNAReview
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Removal of introns from transfer RNA precursors (pre-tRNAs) occurs in all living organisms. This is a vital phase in the maturation and functionality of tRNA. Here we present a 3.2 Å-resolution cryo-EM structure of an active human tRNA splicing endonuclease complex bound to an intron-containing pre-tRNA. TSEN54, along with the unique regions of TSEN34 and TSEN2, cooperatively recognizes the mature body of pre-tRNA and guides the anticodon-intron stem to the correct position for splicing. We capture the moment when the endonucleases are poised for cleavage, illuminating the molecular mechanism for both 3' and 5' cleavage reactions. Two insertion loops from TSEN54 and TSEN2 cover the 3' and 5' splice sites, respectively, trapping the scissile phosphate in the center of the catalytic triad of residues. Our findings reveal the molecular mechanism for eukaryotic pre-tRNA recognition and cleavage, as well as the evolutionary relationship between archaeal and eukaryotic TSENs.
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Registered trials
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