ArticleRNA (New York, N.Y.)2015
Coevolution of RtcB and Archease created a multiple-turnover RNA ligase.
Article in RNA (New York, N.Y.), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Spligation enables programmable chimeric RNA generation in living cells.bioRxiv : the preprint server for biology · 2026Article
- DDX1 is required for non-spliceosomal splicing of tRNAs but not of XBP1 mRNA.Communications biology · 2025Article
- Structural and mechanistic insights into activation of the human RNA ligase RTCB by Archease.Nature communications · 2024Article
- Thioredoxin regulates the redox state and the activity of the human tRNA ligase complex.RNA (New York, N.Y.) · 2023Article
- Insights into the structure and function of the RNA ligase RtcB.Cellular and molecular life sciences : CMLS · 2023Review
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- Regulation of Archease by the mTOR-vATPase axis.Development (Cambridge, England) · 2022Article
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- The Bacterial Ro60 Protein and Its Noncoding Y RNA Regulators.Annual review of microbiology · 2020Review
- Site-Selective RNA Splicing Nanozyme: DNAzyme and RtcB Conjugates on a Gold Nanoparticle.ACS chemical biology · 2018Article
- Functional analysis of the mammalian RNA ligase for IRE1 in the unfolded protein response.Bioscience reports · 2017Article
- RNA damage in biological conflicts and the diversity of responding RNA repair systems.Nucleic acids research · 2016Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
RtcB is a noncanonical RNA ligase that joins either 2',3'-cyclic phosphate or 3'-phosphate termini to 5'-hydroxyl termini. The genes encoding RtcB and Archease constitute a tRNA splicing operon in many organisms. Archease is a cofactor of RtcB that accelerates RNA ligation and alters the NTP specificity of the ligase from Pyrococcus horikoshii. Yet, not all organisms that encode RtcB also encode Archease. Here we sought to understand the differences between Archease-dependent and Archease-independent RtcBs so as to illuminate the evolution of Archease and its function. We report on the Archease-dependent RtcB from Thermus thermophilus and the Archease-independent RtcB from Thermobifida fusca. We find that RtcB from T. thermophilus can catalyze multiple turnovers only in the presence of Archease. Remarkably, Archease from P. horikoshii can activate T. thermophilus RtcB, despite low sequence identity between the Archeases from these two organisms. In contrast, RtcB from T. fusca is a single-turnover enzyme that is unable to be converted into a multiple-turnover ligase by Archease from either P. horikoshii or T. thermophilus. Thus, our data indicate that Archease likely evolved to support multiple-turnover activity of RtcB and that coevolution of the two proteins is necessary for a functional interaction.
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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.