ArticleNature2014
Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors.
Article in Nature, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.
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Who cites it
84 citing papers in PubMed, 126 citations in OpenAlex.
- The cellular landscape of druggable RNA-binding proteins.Nature reviews. Drug discovery · 2026Review
- Structural framework for the assembly of the human tRNA ligase complex.Nature communications · 2026Article
- Ashwin and FAM98 paralogs define nuclear and cytoplasmic RNA ligase complexes for tRNA biogenesis.Nature communications · 2026Article
- RBM39 modulates UPR signaling through alternative splicing of IRE1α/Genes & development · 2026Article
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- Cell-specific variant-to-gene mapping identifies conserved neural and glial regulators of sleep.bioRxiv : the preprint server for biology · 2026Article
- The mitochondrial proteome of diplonemids: from conventional pathways to eccentric RNA editing and transcript processing.BMC genomics · 2025Article
- Trichothiodystrophy-causative pathogenic variants impair a cooperative action of TFIIH and DDX1 in R-loop processing.Nucleic acids research · 2025Article
- Polyglycine-mediated aggregation of FAM98B disrupts tRNA processing in GGC repeat disorders.Science (New York, N.Y.) · 2025Article
- Mechanistic basis for PYROXD1-mediated protection of the human tRNA ligase complex against oxidative inactivation.Nature structural & molecular biology · 2025Article
- A non-syndromic orofacial cleft risk locus links tRNA splicing defects to neural crest cell pathologies.American journal of human genetics · 2025Article
- Structural and biochemical characterization of the 3'-5' tRNA splicing ligases.The Journal of biological chemistry · 2025Article
- Crystallographic analysis of the Escherichia coli tRNA seleno-modification enzyme in complex with tRNA.Acta crystallographica. Section F, Structural biology communications · 2025Article
- Substrate Specificities of DDX1: A Human DEAD-Box Protein.ACS omega · 2025Article
- DDX1 is required for non-spliceosomal splicing of tRNAs but not of XBP1 mRNA.Communications biology · 2025Article
- Article
- RTP801 interacts with the tRNA ligase complex and dysregulates its RNA ligase activity in Alzheimer's disease.Nucleic acids research · 2024Article
- RNA biogenesis and RNA metabolism factors as R-loop suppressors: a hidden role in genome integrity.Genes & development · 2024Review
- Structural and mechanistic insights into activation of the human RNA ligase RTCB by Archease.Nature communications · 2024Article
- Comparative analysis of retroviral Gag-host cell interactions: focus on the nuclear interactome.bioRxiv : the preprint server for biology · 2024Article
24 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
RNA ligases have essential roles in many cellular processes in eukaryotes, archaea and bacteria, including in RNA repair and stress-induced splicing of messenger RNA. In archaea and eukaryotes, RNA ligases also have a role in transfer RNA splicing to generate functional tRNAs required for protein synthesis. We recently identified the human tRNA splicing ligase, a multimeric protein complex with RTCB (also known as HSPC117, C22orf28, FAAP and D10Wsu52e) as the essential subunit. The functions of the additional complex components ASW (also known as C2orf49), CGI-99 (also known as C14orf166), FAM98B and the DEAD-box helicase DDX1 in the context of RNA ligation have remained unclear. Taking advantage of clusters of eukaryotic orthologous groups, here we find that archease (ARCH; also known as ZBTB8OS), a protein of unknown function, is required for full activity of the human tRNA ligase complex and, in cooperation with DDX1, facilitates the formation of an RTCB-guanylate intermediate central to mammalian RNA ligation. Our findings define a role for DDX1 in the context of the human tRNA ligase complex and suggest that the widespread co-occurrence of archease and RtcB proteins implies evolutionary conservation of their functional interplay.
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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.