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Related Concept Videos

Nucleotide Excision Repair01:08

Nucleotide Excision Repair

Overview
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

Overview
Nucleotide Excision Repair01:38

Nucleotide Excision Repair

DNA Distortion and Damage
Cells are regularly exposed to mutagens—factors in the environment that can damage DNA and generate mutations. UV radiation is one of the most common mutagens and is estimated to introduce a significant number of changes in DNA. These include bends or kinks in the structure, which can block DNA replication or transcription. If these errors are not fixed, the damage can cause mutations, which in turn can result in cancer or disease depending on which sequences are...

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Related Experiment Video

Updated: Jun 12, 2026

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes
06:52

Kinetic Screening of Nuclease Activity using Nucleic Acid Probes

Published on: November 1, 2019

A comprehensive screening system for damaged nucleotide-binding proteins.

Daisuke Tsuchimoto1, Teruaki Iyama, Mari Nonaka

  • 1Division of Neurofunctional Genomics, Department of Immunobiology and Neuroscience, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-Ku, Fukuoka 812-8582, Japan. daisuke@bioreg.kyushu-u.ac.jp

Mutation Research
|June 15, 2010
PubMed
Summary
This summary is machine-generated.

A new proteomics screening system identified novel enzymes that remove damaged nucleotides, like inosine triphosphate (ITP). This system validates known enzymes and discovers new ones like NUDT16, crucial for genome stability.

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Area of Science:

  • Biochemistry and Molecular Biology
  • Proteomics
  • Enzymology

Background:

  • Damaged nucleotides, such as inosine triphosphate (ITP), can be harmful to cellular processes.
  • Identifying enzymes that remove these damaged nucleotides is crucial for understanding cellular health and genome stability.
  • Existing methods for identifying such enzymes are limited.

Purpose of the Study:

  • To establish and validate a comprehensive proteomics-based screening system for identifying damaged nucleotide-binding proteins.
  • To discover novel enzymes involved in sanitizing nucleotide pools, with a focus on ITP-binding proteins.
  • To investigate the biochemical functions and cellular roles of newly identified enzymes.

Main Methods:

  • Development of a screening system utilizing affinity chromatography with damaged nucleotide resins for protein purification.
  • Identification of purified proteins using mass spectrometry.
  • Biochemical assays to determine enzyme activity and specificity; cell-based assays (e.g., knockdown) to assess cellular roles.

Main Results:

  • The screening system successfully identified known ITP-hydrolyzing enzymes, inosine triphosphatase (ITPA), validating the system's efficacy.
  • Human nucleoside diphosphate linked moiety X-type motif 16 (NUDT16) was identified as an ITP-binding protein that selectively hydrolyzes deoxyinosine diphosphate (dIDP) and inosine diphosphate (IDP).
  • NUDT16 knockdown led to decreased cell proliferation and increased DNA strand breaks, highlighting its role in genome stability. RS21-C6 was also identified as a dCTP and 5-halo-dCTP hydrolyzing enzyme.

Conclusions:

  • The developed proteomics screening system is effective for identifying damaged nucleotide-binding proteins and enzymes involved in nucleotide pool sanitization.
  • NUDT16 plays a critical role in maintaining genome stability by hydrolyzing specific damaged nucleotides.
  • The screening system provides a valuable tool for studying the health effects of damaged nucleotides and cellular defense mechanisms.