ArticleBMC biology2020
Crystal structure of the yeast heterodimeric ADAT2/3 deaminase.
Article in BMC biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 31 citations in OpenAlex.
- Comparative Analysis of Lifecycle-Dependent A to I RNA Editing in Three Members of theJournal of fungi (Basel, Switzerland) · 2026Article
- Mapping the interactome of human tRNA methyltransferase TRMT1 using dual proximity labeling.bioRxiv : the preprint server for biology · 2026Article
- The tRNA Editing Complex ADAT2/3 Promotes Cancer Cell Growth and Codon-biased mRNA Translation.Journal of molecular biology · 2025Article
- ADAT3 variants disrupt the activity of the ADAT tRNA deaminase complex and impair neuronal migration.Brain : a journal of neurology · 2025Article
- The C-terminal structure of the N6-methyladenosine deaminase YerA and its role in deamination.The Biochemical journal · 2025Article
- Dynamics of diversified A-to-I editing in Streptococcus pyogenes is governed by changes in mRNA stability.Nucleic acids research · 2024Article
- ADATs: roles in tRNA editing and relevance to disease.Acta biochimica et biophysica Sinica · 2024Review
- Unveiling the A-to-I mRNA editing machinery and its regulation and evolution in fungi.Nature communications · 2024Article
- RNA modifications in pulmonary diseases.MedComm · 2024Review
- Sexual stage-specific A-to-I mRNA editing is mediated by tRNA-editing enzymes in fungi.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- RNA editing enzymes: structure, biological functions and applications.Cell & bioscience · 2024Review
- High-Resolution Profiling of Head and Neck Squamous Cells Carcinoma Identifies Specific Biomarkers and Expression Subtypes of Clinically Relevant Vulnerabilities.Current medicinal chemistry · 2024Article
- Epitranscriptomic modifications in mesenchymal stem cell differentiation: advances, mechanistic insights, and beyond.Cell death and differentiation · 2024Review
- Engineered deaminases as a key component of DNA and RNA editing tools.Molecular therapy. Nucleic acids · 2023Review
- Amphioxus adenosine-to-inosine tRNA-editing enzyme that can perform C-to-U and A-to-I deamination of DNA.Communications biology · 2023Article
- The life and times of a tRNA.RNA (New York, N.Y.) · 2023Review
- The occurrence, characteristics, and adaptation of A-to-I RNA editing in bacteria: A review.Frontiers in microbiology · 2023Review
- Structural basis for sequence-independent substrate selection by eukaryotic wobble base tRNA deaminase ADAT2/3.Nature communications · 2022Article
- RNA modifications: importance in immune cell biology and related diseases.Signal transduction and targeted therapy · 2022Review
- The structure of the mouse ADAT2/ADAT3 complex reveals the molecular basis for mammalian tRNA wobble adenosine-to-inosine deamination.Nucleic acids research · 2021Article
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
Abstract
backgroundThe adenosine-to-inosine (A-to-I) editing in anticodons of tRNAs is critical for wobble base-pairing during translation. This modification is produced via deamination on A34 and catalyzed by the adenosine deaminase acting on tRNA (ADAT) enzyme. Eukaryotic ADATs are heterodimers composed of the catalytic subunit ADAT2 and the structural subunit ADAT3, but their molecular assemblies and catalytic mechanisms are largely unclear.
resultsHere, we report a 2.8-Å crystal structure of Saccharomyces cerevisiae ADAT2/3 (ScADAT2/3), revealing its heterodimeric assembly and substrate recognition mechanism. While each subunit clearly contains a domain resembling their prokaryotic homolog TadA, suggesting an evolutionary gene duplication event, they also display accessory domains for additional structural or functional purposes. The N-lobe of ScADAT3 exhibits a positively charged region with a potential role in the recognition and binding of tRNA, supported by our biochemical analysis. Interestingly, ScADAT3 employs its C-terminus to block tRNA's entry into its pseudo-active site and thus inactivates itself for deamination despite the preservation of a zinc-binding site, a mechanism possibly shared only among yeasts.
conclusionsCombining the structural with biochemical, bioinformatic, and in vivo functional studies, we propose a stepwise model for the pathway of deamination by ADAT2/3. Our work provides insight into the molecular mechanism of the A-to-I editing by the eukaryotic ADAT heterodimer, especially the role of ADAT3 in catalysis.
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