ArticleNucleic acids research2015
Recognition of duplex RNA by the deaminase domain of the RNA editing enzyme ADAR2.
Article in Nucleic acids research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed.
- Structural perspectives on adenosine to inosine RNA editing by ADARs.Molecular therapy. Nucleic acids · 2024Review
- RNA sequences that direct selective ADAR editing from a SELEX library bearing 8-azanebularine.Bioorganic & medicinal chemistry · 2024Article
- Impact of Disease-Associated Mutations on the Deaminase Activity of ADAR1.Biochemistry · 2024Article
- Chemical Modifications in RNA: Elucidating the Chemistry of dsRNA-Specific Adenosine Deaminases (ADARs).Accounts of chemical research · 2023Article
- A-to-I RNA editing by ADAR and its therapeutic applications: From viral infections to cancer immunotherapy.Wiley interdisciplinary reviews. RNA · 2023Review
- Genome-wide profiling of rice Double-stranded RNA-Binding Protein 1-associated RNAs by targeted RNA editing.Plant physiology · 2023Article
- Development of a selection assay for small guide RNAs that drive efficient site-directed RNA editing.Nucleic acids research · 2023Article
- Selective Inhibition of ADAR1 Using 8-Azanebularine-Modified RNA Duplexes.Biochemistry · 2023Article
- Programmable RNA editing with endogenous ADAR enzymes - a feasible option for the treatment of inherited retinal disease?Frontiers in molecular neuroscience · 2023Review
- Article
- Biology of the mRNA Splicing Machinery and Its Dysregulation in Cancer Providing Therapeutic Opportunities.International journal of molecular sciences · 2021Review
- Regulation of RNA editing by intracellular acidification.Nucleic acids research · 2021Article
- Evaluation of Engineered CRISPR-Cas-Mediated Systems for Site-Specific RNA Editing.Cell reports · 2020Article
- Chemical Profiling of A-to-I RNA Editing Using a Click-Compatible Phenylacrylamide.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Article
- Suppression of adenosine-to-inosine (A-to-I) RNA editome by death associated protein 3 (DAP3) promotes cancer progression.Science advances · 2020Article
- Novel Engineered Programmable Systems for ADAR-Mediated RNA Editing.Molecular therapy. Nucleic acids · 2020Review
- Current strategies for Site-Directed RNA Editing using ADARs.Methods (San Diego, Calif.) · 2019Review
- A Bump-Hole Approach for Directed RNA Editing.Cell chemical biology · 2019Article
- Implementation of the CRISPR-Cas13a system in fission yeast and its repurposing for precise RNA editing.Nucleic acids research · 2018Article
- All I's on the RADAR: role of ADAR in gene regulation.FEBS letters · 2018Review
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
Adenosine deaminases acting on RNA (ADARs) hydrolytically deaminate adenosines (A) in a wide variety of duplex RNAs and misregulation of editing is correlated with human disease. However, our understanding of reaction selectivity is limited. ADARs are modular enzymes with multiple double-stranded RNA binding domains (dsRBDs) and a catalytic domain. While dsRBD binding is understood, little is known about ADAR catalytic domain/RNA interactions. Here we use a recently discovered RNA substrate that is rapidly deaminated by the isolated human ADAR2 deaminase domain (hADAR2-D) to probe these interactions. We introduced the nucleoside analog 8-azanebularine (8-azaN) into this RNA (and derived constructs) to mechanistically trap the protein-RNA complex without catalytic turnover for EMSA and ribonuclease footprinting analyses. EMSA showed that hADAR2-D requires duplex RNA and is sensitive to 2'-deoxy substitution at nucleotides opposite the editing site, the local sequence and 8-azaN nucleotide positioning on the duplex. Ribonuclease V1 footprinting shows that hADAR2-D protects ∼ 23 nt on the edited strand around the editing site in an asymmetric fashion (∼ 18 nt on the 5' side and ∼ 5 nt on the 3' side). These studies provide a deeper understanding of the ADAR catalytic domain-RNA interaction and new tools for biophysical analysis of ADAR-RNA complexes.
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