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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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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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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
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RAD51AP1 mediates RAD51 activity through nucleosome interaction.

Elena Pires1, Neelam Sharma2, Platon Selemenakis1

  • 1Department of Environmental and Radiological Health Sciences, Colorado State University, Fort Collins, Colorado, USA; Cell and Molecular Biology Graduate Program, Colorado State University, Fort Collins, Colorado, USA.

The Journal of Biological Chemistry
|May 31, 2021
PubMed
Summary

RAD51-associated protein 1 (RAD51AP1) binds to nucleosomes, aiding homologous recombination DNA repair in chromatin. This protein facilitates RAD51

Keywords:
RAD51RAD51AP1chromatinhomologous recombination DNA repairmononucleosomessynaptic complex assembly

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Area of Science:

  • Molecular Biology
  • Genetics
  • Biochemistry

Background:

  • Homologous recombination (HR) is crucial for DNA repair, but chromatin structure presents challenges.
  • RAD51AP1 is a key protein in HR, interacting with RAD51 recombinase.
  • Previous studies showed RAD51AP1's role with nucleosome-free DNA, but its function in chromatin was unclear.

Purpose of the Study:

  • To investigate RAD51AP1's interaction with chromatin.
  • To determine if RAD51AP1 can facilitate HR in the context of nucleosomes.
  • To elucidate the mechanism by which RAD51AP1 functions within chromatin.

Main Methods:

  • Studied RAD51AP1 binding to nucleosome core particles (NCPs) and histone octamers.
  • Identified the C-terminal region of RAD51AP1 responsible for NCP and histone binding.
  • Utilized in vitro surrogate assays to assess HR activity with chromatinized DNA.

Main Results:

  • RAD51AP1 directly binds to NCPs and histone octamers.
  • A C-terminal region of RAD51AP1 is critical for this interaction.
  • RAD51AP1 promotes DNA capture and joint-molecule formation with NCPs and chromatinized DNA in vitro.

Conclusions:

  • RAD51AP1 directly facilitates the RAD51-mediated search for donor DNA within chromatin.
  • RAD51AP1 anchors the DNA template to the RAD51-ssDNA nucleoprotein filament via nucleosome affinity.
  • These findings reveal a novel mechanism for HR in the complex environment of chromatin.