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Counting RAD51 proteins disassembling from nucleoprotein filaments under tension

Author

Listed:
  • Joost van Mameren

    (VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands
    Present address: JPK Instruments AG, Bouchéstrasse 12, 12435 Berlin, Germany.)

  • Mauro Modesti

    (Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands
    CNRS, Unité Propre de Recherche 3081, Genome Instability and Carcinogenesis Conventionné par l'Université d'Aix-Marseille 2, 13402 Marseille Cedex 20, France)

  • Roland Kanaar

    (Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands
    Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands)

  • Claire Wyman

    (Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands
    Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands)

  • Erwin J. G. Peterman

    (VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands)

  • Gijs J. L. Wuite

    (VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands)

Abstract

DNA repair: RAD51 protein disassembly To ensure the correct segregation of chromosomes and during some forms of DNA repair, two homologous DNAs are brought together to swap homologous strands. This process, DNA strand exchange, results in a physical linkage between the two molecules. The RecA/RAD51 family of ATPases mediates strand exchange by forming a long filament on the DNA. One of the unresolved questions in the field is how this filament is disassembled once the strands are exchanged. In this work, van Mameren et al. use a single-molecule approach to elucidate the mechanics of this process and its relationship to the energy released by nucleotide hydrolysis.

Suggested Citation

  • Joost van Mameren & Mauro Modesti & Roland Kanaar & Claire Wyman & Erwin J. G. Peterman & Gijs J. L. Wuite, 2009. "Counting RAD51 proteins disassembling from nucleoprotein filaments under tension," Nature, Nature, vol. 457(7230), pages 745-748, February.
    • Handle: RePEc:nat:nature:v:457:y:2009:i:7230:d:10.1038_nature07581
    DOI: 10.1038/nature07581
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    Cited by:

    1. Shih-Chi Luo & Min-Chi Yeh & Yu-Hsiang Lien & Hsin-Yi Yeh & Huei-Lun Siao & I-Ping Tu & Peter Chi & Meng-Chiao Ho, 2023. "A RAD51–ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    2. Michael A. Longo & Sunetra Roy & Yue Chen & Karl-Heinz Tomaszowski & Andrew S. Arvai & Jordan T. Pepper & Rebecca A. Boisvert & Selvi Kunnimalaiyaan & Caezanne Keshvani & David Schild & Albino Bacolla, 2023. "RAD51C-XRCC3 structure and cancer patient mutations define DNA replication roles," Nature Communications, Nature, vol. 14(1), pages 1-16, December.
    3. Jiaqi Yan & Rajendra Bhadane & Meixin Ran & Xiaodong Ma & Yuanqiang Li & Dongdong Zheng & Outi M. H. Salo-Ahen & Hongbo Zhang, 2024. "Development of Aptamer-DNAzyme based metal-nucleic acid frameworks for gastric cancer therapy," Nature Communications, Nature, vol. 15(1), pages 1-20, December.

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