ArticleNature structural & molecular biology2025
Structure of fungal tRNA ligase Trl1 with RNA reveals conserved substrate-binding principles.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- Many paths to destruction: Family-specific turnover and stress responses for tRNA introns.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- A chimeric rather than native secretion signal elicits stress-related transcriptional adaption during 75k γ-secalin production inFEMS microbes · 2026Article
- MANY PATHS TO DESTRUCTION: FAMILY-SPECIFIC TURNOVER AND STRESS RESPONSES FOR TRNA INTRONS.bioRxiv : the preprint server for biology · 2025Article
- Interdomain assembly between the fungal tRNA ligase adenylyltransferase and kinase domain.RNA (New York, N.Y.) · 2025Article
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Authors and funding
5 authors.
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Abstract
RNA ligases play a vital role in RNA processing and maturation, including tRNA splicing, RNA repair and the unfolded protein response (UPR). In fungi and plants, the tripartite tRNA ligase Trl1 catalyzes the joining of TSEN-cleaved pre-tRNA exon halves. Trl1 also functions as ligase in the non-conventional HAC1 mRNA splicing during the UPR. The final ligation step is performed by the N-terminal adenylyltransferase domain (ligase; LIG). The spatial arrangement of the exon ends during the ligation reaction has remained elusive. Here we report the crystal structure of Chaetomium thermophilum Trl1-LIG in complex with a tRNA-derived substrate. Our structure represents a snapshot of the activated RNA intermediate and defines the conserved substrate-binding interface. The underlying enzyme-substrate interplay reveals a substrate-binding principle shared by adenylyltransferases. Moreover, we identify the determinants of RNA end specificity as well as the specific roles of Trl1-LIG's subdomains during ligase activation, substrate binding and phosphoryl transfer.
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