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Updated: Jul 18, 2025
11:09
Characterizing the Composition of Molecular Motors on Moving Axonal Cargo Using "Cargo Mapping" Analysis
Published on: October 30, 2014
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Holliday junction branch migration driven by AAA+ ATPase motors.
Jiri Wald1, Thomas C Marlovits1
1Centre for Structural Systems Biology, Notkestraße 85, 22607 Hamburg, Germany; Institute of Structural and Systems Biology, University Medical Center Hamburg-Eppendorf, Notkestraße 85, 22607 Hamburg, Germany; Deutsches Elektronen Synchrotron (DESY), Notkestraße 85, 22607 Hamburg, Germany.
Current Opinion in Structural Biology
|August 21, 2023
Summary
The RuvAB complex
Area of Science:
- Molecular Biology
- Structural Biology
- Biochemistry
Background:
- Holliday junctions are crucial intermediates in genetic recombination.
- The bacterial RuvAB complex is a conserved protein complex that processes Holliday junctions via ATP-dependent branch migration.
- Previous technical limitations obscured the detailed structure and mechanism of RuvAB.
Purpose of the Study:
- To elucidate the structure and mechanism of the RuvAB branch migration complex.
- To propose an integrated model for RuvAB-mediated Holliday junction branch migration.
- To reveal the regulatory mechanisms of the AAA+ RuvB ATPase in substrate translocation.
Main Methods:
- Time-resolved cryo-electron microscopy (cryo-EM) was used to resolve structures of a reconstituted RuvAB complex.
- Analysis of distinct conformational states during Holliday junction processing.
Main Results:
- Structures revealed distinct conformational states of RuvAB during branch migration.
- An integrated model for RuvAB Holliday junction branch migration was proposed.
- Novel insights into the coordinated nucleotide cycle of the hexameric RuvB ATPase were obtained.
Conclusions:
- Recent structural studies have clarified the mechanism of RuvAB-mediated branch migration.
- The findings provide a deeper understanding of DNA repair and recombination pathways.
- Future research directions for RuvAB and AAA+ ATPase mechanisms are outlined.
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