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Holthausen, J.T. (author), Van Loenhout, M.T.J. (author), Sanchez, H. (author), Ristic, D. (author), Van Rossum-Fikkert, S.E. (author), Modesti, M. (author), Dekker, C. (author), Kanaar, R. (author), Wyman, C. (author)
Homologous recombination is essential for the preservation of genome stability, thereby preventing cancer. The recombination protein RAD51 drives DNA strand exchange, which requires the assembly, rearrangement and disassembly of a RAD51 filament on DNA, coupled to ATP binding and hydrolysis. This process is facilitated and controlled by...
journal article 2011
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Van der Heijden, T. (author), Seidel, R. (author), Modesti, M. (author), Kanaar, R. (author), Wyman, C. (author), Dekker, C. (author)
The human DNA repair protein RAD51 is the crucial component of helical nucleoprotein filaments that drive homologous recombination. The molecular mechanistic details of how this structure facilitates the requisite DNA strand rearrangements are not known but must involve dynamic interactions between RAD51 and DNA. Here, we report the real-time...
journal article 2007
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Ristic, D. (author), Modesti, M. (author), Van der Heijden, T. (author), Van Noort, J. (author), Dekker, C. (author), Kanaar, R. (author), Wyman, C. (author)
Recombinase proteins assembled into helical filaments on DNA are believed to be the catalytic core of homologous recombination. The assembly, disassembly and dynamic rearrangements of this structure must drive the DNA strand exchange reactions of homologous recombination. The sensitivity of eukaryotic recombinase activity to reaction conditions...
journal article