ArticleNucleic acids research2012
Nucleoside analog studies indicate mechanistic differences between RNA-editing adenosine deaminases.
Article in Nucleic acids research, 2012. 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, 23 citations in OpenAlex.
- Regulation of RNA editing by intracellular acidification.Nucleic acids research · 2021Article
- ADARs, RNA editing and more in hematological malignancies.Leukemia · 2021Review
- Review
- Nucleoside analogs in the study of the epitranscriptome.Methods (San Diego, Calif.) · 2019Review
- DNA editing in DNA/RNA hybrids by adenosine deaminases that act on RNA.Nucleic acids research · 2017Article
- An efficient system for selectively altering genetic information within mRNAs.Nucleic acids research · 2016Article
- Nearest-neighbor parameters for 7-deaza-adenosine·uridine base pairs in RNA duplexes.RNA (New York, N.Y.) · 2016Article
- Editing of Cellular Self-RNAs by Adenosine Deaminase ADAR1 Suppresses Innate Immune Stress Responses.The Journal of biological chemistry · 2016Article
- New Insights into the Biological Role of Mammalian ADARs; the RNA Editing Proteins.Biomolecules · 2015Review
- A Fluorescent Adenosine Analogue as a Substrate for an A-to-I RNA Editing Enzyme.Angewandte Chemie (International ed. in English) · 2015Article
- Recognition of duplex RNA by the deaminase domain of the RNA editing enzyme ADAR2.Nucleic acids research · 2015Article
- Click modification of RNA at adenosine: structure and reactivity of 7-ethynyl- and 7-triazolyl-8-aza-7-deazaadenosine in RNA.ACS chemical biology · 2014Article
- Potent and selective inhibition of A-to-I RNA editing with 2'-O-methyl/locked nucleic acid-containing antisense oligoribonucleotides.ACS chemical biology · 2013Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Adenosine deaminases acting on RNA (ADAR1 and ADAR2) are human RNA-editing adenosine deaminases responsible for the conversion of adenosine to inosine at specific locations in cellular RNAs. Since inosine is recognized during translation as guanosine, this often results in the expression of protein sequences different from those encoded in the genome. While our knowledge of the ADAR2 structure and catalytic mechanism has grown over the years, our knowledge of ADAR1 has lagged. This is due, at least in part, to the lack of well defined, small RNA substrates useful for mechanistic studies of ADAR1. Here, we describe an ADAR1 substrate RNA that can be prepared by a combination of chemical synthesis and enzymatic ligation. Incorporation of adenosine analogs into this RNA and analysis of the rate of ADAR1 catalyzed deamination revealed similarities and differences in the way the ADARs recognize the edited nucleotide. Importantly, ADAR1 is more dependent than ADAR2 on the presence of N7 in the edited base. This difference between ADAR1 and ADAR2 appears to be dependent on the identity of a single amino acid residue near the active site. Thus, this work provides an important starting point in defining mechanistic differences between two functionally distinct human RNA editing ADARs.
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Registered trials
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