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Nucleic Acids Research Advance Access originally published online on June 12, 2007
Nucleic Acids Research 2007 35(12):4124-4140; doi:10.1093/nar/gkm412
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Nucleic Acids Research, 2007, Vol. 35, No. 12 4124-4140
© 2007 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Nucleic Acid Enzymes

Rad51 and Rad54 ATPase activities are both required to modulate Rad51-dsDNA filament dynamics

Xuan Li1, Xiao-Ping Zhang1, Jachen A. Solinger1, Konstantin Kiianitsa1, Xiong Yu2, Edward H. Egelman2 and Wolf-Dietrich Heyer1,3,*

1Section of Microbiology, University of California, Davis, CA 95616-8665, 2Department of Biochemistry and Molecular Genetics, University of Virginia, Charlottesville, VA 22908 and 3Section of Molecular and Cellular Biology, University of California, Davis, CA 95616-8665, USA

*To whom correspondence should be addressed. Tel.: 530 752 3001; Fax: 530 752 3011; Email: wdheyer{at}ucdavis.edu

Received April 3, 2007. Revised May 3, 2007. Accepted May 4, 2007.

Rad51 and Rad54 are key proteins that collaborate during homologous recombination. Rad51 forms a presynaptic filament with ATP and ssDNA active in homology search and DNA strand exchange, but the precise role of its ATPase activity is poorly understood. Rad54 is an ATP-dependent dsDNA motor protein that can dissociate Rad51 from dsDNA, the product complex of DNA strand exchange. Kinetic analysis of the budding yeast proteins revealed that the catalytic efficiency of the Rad54 ATPase was stimulated by partial filaments of wild-type and Rad51-K191R mutant protein on dsDNA, unambiguously demonstrating that the Rad54 ATPase activity is stimulated under these conditions. Experiments with Rad51-K191R as well as with wild-type Rad51-dsDNA filaments formed in the presence of ATP, ADP or ATP-{gamma}-S showed that efficient Rad51 turnover from dsDNA requires both the Rad51 ATPase and the Rad54 ATPase activities. The results with Rad51-K191R mutant protein also revealed an unexpected defect in binding to DNA. Once formed, Rad51-K191R-DNA filaments appeared normal upon electron microscopic inspection, but displayed significantly increased stability. These biochemical defects in the Rad51-K191R protein could lead to deficiencies in presynapsis (filament formation) and postsynapsis (filament disassembly) in vivo.

Present address: Jachen A. Solinger, IFOM-FIRC Institute of Molecular Oncology, I-20139, Milano, Italy and Konstantin Kiianitsa, Fred Hutchinson Cancer Research Center, Seattle, WA 98109-1024, USA.


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