ArticleNature communications2024
Structural and mechanistic insights into activation of the human RNA ligase RTCB by Archease.
Article in Nature communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Detection and sequencing of ApProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Ashwin and FAM98 paralogs define nuclear and cytoplasmic RNA ligase complexes for tRNA biogenesis.Nature communications · 2026Article
- Structural framework for the assembly of the human tRNA ligase complex.Nature communications · 2026Article
- The regulation, function and disease relevance of cytoplasmic tRNAs.Nature reviews. Molecular cell biology · 2026Review
- Enzymology of the metazoan tRNA ligase complex: a lifetime in cycles.Cellular and molecular life sciences : CMLS · 2026Review
- Mechanistic basis for PYROXD1-mediated protection of the human tRNA ligase complex against oxidative inactivation.Nature structural & molecular biology · 2025Article
- Structural and biochemical characterization of the 3'-5' tRNA splicing ligases.The Journal of biological chemistry · 2025Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
RNA ligases of the RTCB-type play an essential role in tRNA splicing, the unfolded protein response and RNA repair. RTCB is the catalytic subunit of the pentameric human tRNA ligase complex. RNA ligation by the tRNA ligase complex requires GTP-dependent activation of RTCB. This active site guanylylation reaction relies on the activation factor Archease. The mechanistic interplay between both proteins has remained unknown. Here, we report a biochemical and structural analysis of the human RTCB-Archease complex in the pre- and post-activation state. Archease reaches into the active site of RTCB and promotes the formation of a covalent RTCB-GMP intermediate through coordination of GTP and metal ions. During the activation reaction, Archease prevents futile RNA substrate binding to RTCB. Moreover, monomer structures of Archease and RTCB reveal additional states within the RNA ligation mechanism. Taken together, we present structural snapshots along the reaction cycle of the human tRNA ligase.
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