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Related Experiment Videos

Structure and subunit composition of the RuvAB-Holliday junction complex

X Yu1, S C West, E H Egelman

  • 1Department of Cell Biology and Neuroanatomy, University of Minnesota Medical School, Minneapolis 55455, USA.

Journal of Molecular Biology
|February 21, 1997
PubMed
Summary

The E. coli RuvA and RuvB proteins bind to DNA Holliday junctions, facilitating repair and recombination. Structural analysis reveals a model where RuvB pumps DNA through its rings during branch migration.

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • DNA Repair

Background:

  • DNA recombination and repair are crucial for genomic stability.
  • The E. coli RuvA and RuvB proteins are key players in resolving Holliday junctions.
  • Understanding their mechanism is vital for comprehending DNA repair pathways.

Purpose of the Study:

  • To elucidate the structural basis of RuvA and RuvB function at Holliday junctions.
  • To propose a model for DNA branch migration mediated by these proteins.

Main Methods:

  • Electron microscopy and image analysis were employed.
  • Structural examination of RuvA and RuvB bound to model Holliday structures.
  • Mass analysis of the RuvAB-junction complex.

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Main Results:

  • RuvB forms bipolar hexameric rings with large ends facing the junction.
  • A model suggests DNA is pumped from RuvB's small end during ATP hydrolysis.
  • Two RuvA tetramers form a symmetrical sandwich around the Holliday junction.

Conclusions:

  • The study provides a structural model for DNA branch migration.
  • The findings offer insights into the coordinated action of RuvA and RuvB in DNA repair.
  • Structural polarity in RuvB is conserved in other helicases like bacteriophage T7 gp4.