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Related Experiment Video

Updated: May 13, 2026

Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates

Nonradioactive Assay to Measure Polynucleotide Phosphorylation of Small Nucleotide Substrates

Published on: May 8, 2020

Catalytic DNA with phosphatase activity.

Jagadeeswaran Chandrasekar¹, Scott K Silverman

¹Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.

Proceedings of the National Academy of Sciences of the United States of America

|March 20, 2013

Summary

This summary is machine-generated.

DNAzymes, or DNA enzymes, can now perform phosphatase activity, catalyzing the hydrolysis of phosphoserine and phosphotyrosine. This breakthrough significantly enhances DNA catalysis, enabling applications as artificial phosphatases.

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Area of Science:

Biochemistry
Molecular Biology
Synthetic Biology

Background:

Catalytic DNA sequences, known as deoxyribozymes or DNAzymes, are engineered for diverse catalytic functions through in vitro selection.
Expanding the scope of DNA catalysis is crucial for fundamental understanding and practical applications, especially from unbiased sequence pools.

Purpose of the Study:

To investigate and demonstrate the capability of DNA sequences to catalyze phosphomonoester hydrolysis, exhibiting phosphatase activity.
To identify novel DNAzymes with enhanced phosphatase activity and explore their substrate specificity and catalytic efficiency.

Main Methods:

In vitro selection was employed to identify DNA sequences with catalytic phosphatase activity.
Kinetic assays were performed to quantify the catalytic efficiency, including the reduction in half-life for phosphoserine hydrolysis.
Substrate specificity was assessed using both phosphopeptide and non-peptidic substrates.

Main Results:

Novel DNAzymes were identified that exhibit significant Zn(2+)-dependent phosphatase activity, catalyzing the hydrolysis of phosphoserine and phosphotyrosine.
The most effective deoxyribozyme reduced the half-life of phosphoserine hydrolysis from over 10^10 years to less than 1 hour.
The DNAzymes showed a preference for phosphopeptide substrates over non-peptidic ones and demonstrated multiple turnover capabilities.

Conclusions:

DNAzymes can be engineered to function as artificial phosphatases with high efficiency, particularly for phosphopeptide substrates.
The identified DNA catalysts are active in complex biological environments like cell lysate and can dephosphorylate larger protein substrates.
These findings suggest broad potential applications for DNA catalysts in biological and biotechnological contexts, mimicking natural phosphatase functions.