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Related Concept Videos

Homologous Recombination02:31

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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

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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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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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Base Excision Repair01:54

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One of the common DNA damages is the chemical alteration of single bases by alkylation, oxidation, or deamination. The altered bases cause mispairing and strand breakage during replication. This type of damage causes minimal change to the DNA double helix structure and can be repaired by the base excision repair (BER) pathways. BER corrects damaged DNA sequences by removing the damaged base and restoring the original base sequence using the complementary strand as a template.
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Visualization of DNA Repair Proteins Interaction by Immunofluorescence
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Rad51 determines pathway usage in post-replication repair.

Damon Meyer, Shannon J Ceballos, Steven Gore

    Biorxiv : the Preprint Server for Biology
    |June 25, 2024
    PubMed
    Summary
    This summary is machine-generated.

    New mutations in Rad51 protein reveal its dual role in DNA repair. Rad51

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    Area of Science:

    • Molecular Biology
    • Genetics
    • Biochemistry

    Background:

    • Stalled replication forks require post-replication repair (PRR) mechanisms, including homologous recombination (HR), fork regression, and translesion DNA synthesis.
    • The Rad51 protein is crucial for genomic stability, participating in HR and protecting stalled forks from degradation.
    • Regulation governing the choice between PRR pathways remains incompletely understood.

    Purpose of the Study:

    • To investigate the role of Rad51 in regulating pathway usage during post-replication repair.
    • To identify and characterize separation-of-function mutations in Rad51 affecting fork protection but not recombination.
    • To elucidate the structural and mechanistic basis of Rad51's function in stalled replication fork processing.

    Main Methods:

    • Isolation and characterization of separation-of-function mutations in Saccharomyces cerevisiae Rad51.
    • In vivo and in vitro assays to assess recombination proficiency, DNA binding, ATPase activity, and fork protection.
    • High-resolution cryo-electron microscopy to determine the structure of Rad51-ssDNA filaments.

    Main Results:

    • Identified Rad51 mutations (Rad51-E135D, Rad51-K305N) with normal recombination but defective fork protection.
    • Mutants exhibited altered DNA binding profiles, particularly to double-stranded DNA (dsDNA), impacting ATPase activity.
    • Demonstrated impaired Rad51 recruitment to stalled forks and reduced protection of dsDNA from nucleases (Dna2-Sgs1, Exo1) in vitro.
    • Determined a high-resolution cryo-electron microscopy structure of the Rad51-ssDNA filament.

    Conclusions:

    • Rad51's ability to bind duplex DNA is critical for controlling pathway selection at stalled replication forks.
    • Defects in Rad51's fork protection function shift post-replication repair usage towards alternative, potentially mutagenic, pathways.
    • These findings provide a mechanistic understanding of Rad51's multifaceted roles in maintaining genomic integrity.