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Related Experiment Videos

SSB protein limits RecOR binding onto single-stranded DNA.

Michael D Hobbs1, Akiko Sakai, Michael M Cox

  • 1Department of Biochemistry, University of Wisconsin, Madison, Wisconsin 53706-1544, USA.

The Journal of Biological Chemistry
|February 3, 2007
PubMed
Summary
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The RecOR protein complex

Area of Science:

  • Molecular Biology
  • DNA Repair Mechanisms
  • Protein-DNA Interactions

Background:

  • The RecOR protein complex is crucial for initiating RecA filament formation on single-stranded DNA (ssDNA).
  • RecA loading onto SSB-coated ssDNA is a key step in DNA repair pathways.
  • Previous studies noted optimal RecOR concentrations but observed slow RecA loading kinetics.

Purpose of the Study:

  • To investigate the rate-limiting step in RecOR-promoted RecA nucleation onto ssDNA.
  • To elucidate the inhibitory role of SSB protein in RecOR-mediated RecA loading.
  • To understand the specific contribution of SSB's C-terminus to RecOR binding and function.

Main Methods:

  • In vitro biochemical assays to monitor RecA filament formation.
  • Kinetic analysis of RecOR protein binding to ssDNA in the presence and absence of SSB.

Related Experiment Videos

  • Utilizing a variant of SSB protein lacking its C-terminal 8 amino acids.

    • Main Results:

    • RecOR-mediated RecA loading onto ssDNA exhibits a significant lag phase, indicating a slow initial step.
    • SSB protein inhibits the binding of RecOR to ssDNA, despite known RecO-SSB interactions.
    • Preincubation of RecOR with ssDNA before SSB addition restores RecA loading efficiency.
    • The C-terminal region of SSB is essential for the inhibitory effect on RecOR binding.

    Conclusions:

    • The binding of RecOR to SSB-coated ssDNA is the rate-limiting step for RecA nucleation.
    • SSB protein, particularly its C-terminus, actively inhibits RecOR's ability to load RecA onto ssDNA.
    • These findings necessitate an updated model for RecOR's function in RecA loading and DNA repair.