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Related Concept Videos

Homologous Recombination02:31

Homologous Recombination

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...
Homologous Recombination02:31

Homologous Recombination

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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Conservative Site-specific Recombination and Phase Variation

Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Restarting Stalled Replication Forks02:37

Restarting Stalled Replication Forks

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, a...
Conserved Binding Sites01:49

Conserved Binding Sites

Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Conserved Binding Sites01:49

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
06:24

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51

Published on: February 13, 2019

Nuclear matrix binding site in the Rad51 recombinase.

Emil V Mladenov1, Peter S Kalev, Boyka B Anachkova

  • 1Institute of Molecular Biology, Bulgarian Academy of Sciences, Sofia, Bulgaria.

Journal of Cellular Physiology
|December 20, 2008
PubMed
Summary

The study identified a nuclear matrix targeting signal in Rad51, crucial for DNA repair foci formation. Deleting this signal prevented Rad51 from forming foci, suggesting nuclear matrix association aids homologous recombination repair.

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Area of Science:

  • Molecular Biology
  • Cell Biology
  • Genetics

Background:

  • The protein Rad51 is essential for homologous recombination repair of DNA damage.
  • Rad51 forms nuclear foci at sites of DNA damage, which are associated with the nuclear matrix.

Purpose of the Study:

  • To investigate if Rad51 possesses a functional domain responsible for its binding to the nuclear matrix.
  • To determine the role of this putative domain in the formation of DNA damage-induced Rad51 foci.

Main Methods:

  • Sequence alignment identified a putative nuclear matrix targeting signal in Rad51.
  • A mutated Rad51 gene, lacking 18 base pairs encoding hydrophobic amino acids in this signal, was created.
  • HeLa cells transfected with wild-type and mutated Rad51 were treated with mitomycin C to assess foci formation and nuclear matrix association.

Main Results:

  • Wild-type Rad51 formed foci attached to the nuclear matrix after DNA damage induction.
  • Mutated Rad51, lacking the putative targeting signal, failed to form DNA damage-induced nuclear foci.
  • The mutation did not impair Rad51's ability to bind double-stranded DNA or chromatin.

Conclusions:

  • The nuclear matrix targeting signal is essential for Rad51's assembly into DNA damage-induced foci.
  • Association with the nuclear matrix likely facilitates the spatial organization of homologous recombination repair.