ArticleNucleic acids research2019
From general base to general acid catalysis in a sodium-specific DNAzyme by a guanine-to-adenine mutation.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 36 citations in OpenAlex.
- SequenceCraft: machine learning-based resource for exploratory analysis of RNA-cleaving deoxyribozymes.BMC bioinformatics · 2025Article
- DNA Catalysis: Design, Function, and Optimization.Molecules (Basel, Switzerland) · 2024Review
- Diaminopurine in Nonenzymatic RNA Template Copying.Journal of the American Chemical Society · 2024Article
- A computational approach to identify efficient RNA cleaving 10-23 DNAzymes.NAR genomics and bioinformatics · 2023Article
- Fluorescent Aptasensor for Highly Specific Detection of ATP Using a Newly Screened Aptamer.Sensors (Basel, Switzerland) · 2022Article
- Rapid detection ofFood science & nutrition · 2021Article
- Wavelength-Selective Activation of Photocaged DNAzymes for Metal Ion Sensing in Live Cells.ACS omega · 2021Article
- Biosensors for Point Mutation Detection.Frontiers in bioengineering and biotechnology · 2021Article
- In vitro Selection of Chemically Modified DNAzymes.ChemistryOpen · 2020Review
- New Deoxyribozymes for the Native Ligation of RNA.Molecules (Basel, Switzerland) · 2020Article
- Engineering base-excised aptamers for highly specific recognition of adenosine.Chemical science · 2020Article
- Catalytic Nucleic Acids: Biochemistry, Chemical Biology, Biosensors, and Nanotechnology.iScience · 2020Review
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4 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Recently, a few Na+-specific RNA-cleaving DNAzymes were reported, where nucleobases are likely to play critical roles in catalysis. The NaA43 and NaH1 DNAzymes share the same 16-nt Na+-binding motif, but differ in one or two nucleotides in a small catalytic loop. Nevertheless, they display an opposite pH-dependency, implicating distinct catalytic mechanisms. In this work, rational mutation studies locate a catalytic adenine residue, A22, in NaH1, while previous studies found a guanine (G23) to be important for the catalysis of NaA43. Mutation with pKa-perturbed analogs, such as 2-aminopurine (∼3.8), 2,6-diaminopurine (∼5.6) and hypoxanthine (∼8.7) affected the overall reaction rate. Therefore, we propose that the N1 position of G23 (pKa ∼6.6) in NaA43 functions as a general base, while that of A22 (pKa ∼6.3) in NaH1 as a general acid. Further experiments with base analogs and a phosphorothioate-modified substrate suggest that the exocyclic amine in A22 and both of the non-bridging oxygens at the scissile phosphate are important for catalysis for NaH1. This is an interesting example where single point mutations can change the mechanism of cleavage from general base to general acid, and it can also explain this Na+-dependent DNAzyme scaffold being sensitive to a broad range of metal ions and molecules.
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