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Related Concept Videos

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...
Nucleotide Excision Repair01:08

Nucleotide Excision Repair

Overview
Mismatch Repair01:20

Mismatch Repair

Organisms are capable of detecting and fixing nucleotide mismatches that occur during DNA replication. This sophisticated process requires identifying the new strand and replacing the erroneous bases with correct nucleotides. Mismatch repair is coordinated by many proteins in both prokaryotes and eukaryotes.
The Mutator Protein Family Plays a Key Role in DNA Mismatch Repair
The human genome has more than 3 billion base pairs of DNA per cell. Prior to cell division, that vast amount of genetic...
Mismatch Repair01:36

Mismatch Repair

Overview
RNA Editing02:23

RNA Editing

RNA editing is a post-transcriptional modification where a precursor mRNA (pre-mRNA) nucleotide sequence is changed by base insertion, deletion, or modification. The extent of RNA editing varies from a few hundred bases, in mitochondrial DNA of trypanosomes, to a just single base, in nuclear genes of mammals. Even a single base change in the pre-mRNA can convert a codon for one amino acid into the codon for another amino acid or a stop codon. This type of re-coding can significantly affect the...

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Related Experiment Video

Updated: Jun 4, 2026

Uracil-DNA Glycosylase Assay by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry Analysis
12:19

Uracil-DNA Glycosylase Assay by Matrix-assisted Laser Desorption/Ionization Time-of-flight Mass Spectrometry Analysis

Published on: April 22, 2022

Structural basis for uracil removal from DNA by human SMUG1.

Julian M Ludäscher1, Emma Scaletti Hutchinson1, Guillem Vila-Julià2

  • 1Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.

Nature Communications
|June 2, 2026
PubMed
Summary

Human SMUG1 enzyme repairs DNA by removing uracil, crucial for genomic integrity and cancer biology. Structural studies reveal its mechanism for base excision, aiding future drug development.

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Published on: August 22, 2019

Area of Science:

  • Molecular Biology
  • Structural Biology
  • Genomics

Background:

  • Human single-strand-selective monofunctional uracil DNA glycosylase 1 (hSMUG1) initiates base excision repair (BER) by removing uracil, 5-hydroxymethyluracil (5hmU), and 5-fluorouracil (5FU) from DNA.
  • hSMUG1 is vital for maintaining genomic integrity and implicated in cancer biology.

Purpose of the Study:

  • To elucidate the structural and mechanistic basis of hSMUG1 activity.
  • To provide insights for developing hSMUG1-targeted inhibitors or activators.

Main Methods:

  • X-ray crystallography to determine structures of hSMUG1 complexes.
  • Molecular dynamics simulations.
  • Neutron diffraction analysis.

Main Results:

  • Presented structures of hSMUG1, including complexes with uracil, 5FU, and double-stranded DNA (dsDNA).
  • Revealed the mechanism of uracil "flipping out" from dsDNA for excision.
  • Identified key residues critical for DNA binding and enzymatic function.
  • Suggested a base excision mechanism involving substrate uracil rotation.

Conclusions:

  • Structural and functional data provide a detailed understanding of hSMUG1's role in DNA repair.
  • Findings are valuable for the rational design of therapeutic agents targeting hSMUG1 in cancer treatment.