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Nucleic Acids Research Advance Access originally published online on December 9, 2008
Nucleic Acids Research 2009 37(2):557-567; doi:10.1093/nar/gkn973
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Nucleic Acids Research, 2009, Vol. 37, No. 2 557-567
© 2008 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.

Genome integrity, repair and replication

Inter-subunit interactions that coordinate Rad51's activities

Arabela A. Grigorescu1, Joseph H. A. Vissers1, Dejan Ristic2, Ying Z. Pigli1, Thomas W. Lynch1, Claire Wyman2 and Phoebe A. Rice1,*

1Department of Biochemistry, Molecular Biology and Cell Biology, The University of Chicago, Chicago, IL 60637 USA and 2Department of Cell Biology and Genetics, and Department of Radiation Oncology, Erasmus University Medical Center, PO BOX 2040, 3000 CA Rotterdam, The Netherlands

*To whom correspondence should be addressed. Tel: +1 773 834 1723; Fax: +1 773 702 0439; Email: price{at}uchicago.edu

Received September 1, 2008. Revised November 13, 2008. Accepted November 18, 2008.

Rad51 is the central catalyst of homologous recombination in eukaryotes and is thus critical for maintaining genomic integrity. Recent crystal structures of filaments formed by Rad51 and the closely related archeal RadA and eubacterial RecA proteins place the ATPase site at the protomeric interface. To test the relevance of this feature, we mutated conserved residues at this interface and examined their effects on key activities of Rad51: ssDNA-stimulated ATP hydrolysis, DNA binding, polymerization on DNA substrates and catalysis of strand-exchange reactions. Our results show that the interface seen in the crystal structures is very important for nucleoprotein filament formation. H352 and R357 of yeast Rad51 are essential for assembling the catalytically competent form of the enzyme on DNA substrates and coordinating its activities. However, contrary to some previous suggestions, neither of these residues is critical for ATP hydrolysis.

Present addresses: Joseph H. A. Vissers, Division of Molecular Genetics and Center for Biomedical Genetics, Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands

Thomas W. Lynch, Caden Biosciences, Madison, WI 53711, USA

Arabela A. Grigorescu, Northwestern University, Evanston, IL, USA


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