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Related Concept Videos

Single-Strand DNA Binding Proteins01:03

Single-Strand DNA Binding Proteins

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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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Fixing Double-strand Breaks02:04

Fixing Double-strand Breaks

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The double-stranded structure of DNA has two major advantages. First, it serves as a safe repository of genetic information where one strand serves as the back-up in case the other strand is damaged. Second, the double-helical structure can be wrapped around proteins called histones to form nucleosomes, which can then be tightly wound to form chromosomes. This way, DNA chains up to 2 inches long can be contained within microscopic structures in a cell. A double-stranded break not only damages...
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Homologous Recombination02:31

Homologous Recombination

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The basic reaction of homologous recombination (HR) involves two chromatids that contain DNA sequences sharing a significant stretch of identity. One of these sequences uses a strand from another as a template to synthesize DNA in an enzyme-catalyzed reaction. The final product is a novel amalgamation of the two substrates. To ensure an accurate recombination of sequences, HR is restricted to the S and G2 phases of the cell cycle. At these stages, the DNA has been replicated already and the...
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Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

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DNA replication is initiated at sites containing predefined DNA sequences known as origins of replication. DNA is unwound at these sites by the minichromosome maintenance (MCM) helicase and other factors such as Cdc45 and the associated GINS complex.The unwound single strands are protected by replication protein A (RPA) until DNA polymerase starts synthesizing DNA at the 5’ end of the strand in the same direction as the replication fork. To prevent the replication fork from falling apart,...
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FISH - Fluorescent In-situ Hybridization02:07

FISH - Fluorescent In-situ Hybridization

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Fluorescence in situ hybridization, or FISH, was developed in the early 1980s and has quickly become one of the most widely used techniques in cytogenetics. Labeled probes are used to bind complementary DNA or RNA sequences on a chromosome or in a region within a cell. Earlier, the probes could only be obtained by cloning or reverse transcription of a DNA template. Currently, the probe oligonucleotides can be synthesized synthetically. Additionally, with the advancement of optical techniques,...
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Base-pairing and DNA Repair02:27

Base-pairing and DNA Repair

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Related Experiment Video

Updated: Jun 18, 2025

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
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Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1

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FANCD2-FANCI surveys DNA and recognizes double- to single-stranded junctions.

Pablo Alcón1, Artur P Kaczmarczyk2,3, Korak Kumar Ray2,3

  • 1MRC Laboratory of Molecular Biology, Cambridge, UK.

Nature
|July 31, 2024
PubMed
Summary
This summary is machine-generated.

The FANCD2-FANCI (D2-I) complex acts as a sliding clamp, identifying DNA damage by stalling at single-stranded-double-stranded junctions at stalled replication forks to initiate repair.

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Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
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Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
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Related Experiment Videos

Last Updated: Jun 18, 2025

Single-Molecule Förster Resonance Energy Transfer Methods for Real-Time Investigation of the Holliday Junction Resolution by GEN1
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Atomic Force Microscopy Investigations of DNA Lesion Recognition in Nucleotide Excision Repair
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Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA
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Single-Molecule Imaging of EWS-FLI1 Condensates Assembling on DNA

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Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Cellular Biology

Background:

  • DNA crosslinks impede DNA replication and are repaired via the Fanconi anemia pathway.
  • The FANCD2-FANCI (D2-I) complex is crucial for initiating DNA repair at crosslink lesions.
  • The D2-I complex also plays a general role in DNA repair and protects stalled replication forks from degradation.

Purpose of the Study:

  • To elucidate the mechanism of DNA crosslink recognition by the D2-I complex.
  • To understand how the D2-I complex functions in protecting stalled replication forks.
  • To reconcile the dual roles of D2-I in DNA repair and replication fork protection.

Main Methods:

  • Single-molecule imaging to observe D2-I dynamics on DNA.
  • Cryogenic electron microscopy (cryo-EM) to determine D2-I-DNA complex structures.
  • Analysis of D2-I interactions with double-stranded DNA and single-stranded-double-stranded junctions.

Main Results:

  • D2-I functions as a sliding clamp that diffuses along double-stranded DNA.
  • D2-I specifically stalls upon encountering single-stranded-double-stranded DNA junctions, characteristic of stalled replication forks.
  • Structural analysis revealed distinct D2-I interactions with ss-dsDNA junctions compared to dsDNA, enabling damage site recognition.

Conclusions:

  • D2-I identifies DNA damage sites by recognizing and clamping onto ss-dsDNA junctions at stalled replication forks.
  • This mechanism provides a unified understanding of D2-I's roles in DNA repair and replication fork protection.
  • The findings offer insights into Fanconi anemia pathway and broader DNA damage response mechanisms.