Counting RAD51 proteins disassembling from nucleoprotein filaments under tension

Joost van Mameren, Mauro Modesti, Roland Kanaar, Claire Wyman, Erwin J. G. Peterman () and Gijs J. L. Wuite ()
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Joost van Mameren: VU University, De Boelelaan 1081, 1081 HV, Amsterdam, The Netherlands
Mauro Modesti: Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands
Roland Kanaar: Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands
Claire Wyman: 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

Nature, 2009, vol. 457, issue 7230, 745-748

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.

Date: 2009
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DOI: 10.1038/nature07581

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