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Related Concept Videos

DNA Damage can Stall the Cell Cycle02:36

DNA Damage can Stall the Cell Cycle

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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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In response to DNA damage, cells can pause the cell cycle to assess and repair the breaks. However, the cell must check the DNA at certain critical stages during the cell cycle. If the cell cycle pauses before DNA replication, the cells will contain twice the amount of DNA. On the other hand, if cells arrest after DNA replication but before mitosis, they will contain four times the normal amount of DNA. With a host of specialized proteins at their disposal,cells must use the right protein at...
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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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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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Since the discovery of the two BER pathways, there has been a debate about how a cell chooses one pathway over the other and the factors determining this selection. Numerous in vitro experiments have pointed out multiple determinants for the sub-pathway selection. These are:
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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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Updated: Mar 30, 2026

Analyzing DNA-Protein Interactions with Streptavidin-Based Biolayer Interferometry
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Structural basis for the recognition of DNA repair proteins UNG2, XPA, and RAD52 by replication factor RPA.

G Mer1, A Bochkarev, R Gupta

  • 1Department of Molecular Biology, The Scripps Research Institute, La Jolla, California 92037, USA.

Cell
|November 18, 2000
PubMed
Summary

Replication protein A (RPA) links DNA repair pathways via its RPA32 subunit. This protein structure reveals a common interaction surface for UNG2, XPA, and RAD52, coordinating DNA repair.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Biochemistry

Background:

  • Replication protein A (RPA) is a crucial nuclear ssDNA-binding protein in eukaryotes.
  • RPA plays essential roles in DNA replication, recombination, and repair processes.

Purpose of the Study:

  • To investigate the structural basis of RPA's interaction with different DNA repair factors.
  • To elucidate how RPA coordinates diverse DNA repair pathways.

Main Methods:

  • Nuclear Magnetic Resonance (NMR) spectroscopy was used to determine the structures.
  • Structural analysis of the RPA32 C-terminal domain, free and bound to UNG2.

Main Results:

  • A specific surface on the RPA32 C-terminal domain interacts with UNG2, XPA, and RAD52.
  • This interaction surface provides a common structural basis for linking RPA to multiple DNA repair pathways.
  • NMR structures revealed the complex formation between the RPA32 domain and the UNG2 interaction domain.

Conclusions:

  • RPA acts as a central coordinator in DNA repair by interacting with factors from different pathways.
  • Findings support a hand-off model for assembling and coordinating DNA repair machinery.
  • The study defines a common structural mechanism for RPA's role in DNA repair.