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Nucleic Acids Research Advance Access published online on June 4, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn352
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© 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.

Molecular Biology

A comparative analysis of Dmc1 and Rad51 nucleoprotein filaments

Sean D. Sheridan1, Xiong Yu2, Robyn Roth3, John E. Heuser3, Michael G. Sehorn4, Patrick Sung4, Edward H. Egelman2 and Douglas K. Bishop1,5,*

1Committee on Genetics, University of Chicago, Chicago, IL 60637, 2Department of Biochemistry and Molecular Genetics, University of Virginia Health Sciences Center, Charlottesville, VA 22908-0733, 3Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, MO 63110, 4Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, CT 06520 and 5Department of Molecular Genetics and Cell Biology, University of Chicago, Chicago, IL 60637, USA

*To whom correspondence should be addressed. Tel: +1 773 702 9211; Fax: +1 773 834 9064; Email: dbishop{at}midway.uchicago.edu

Received April 3, 2008. Revised May 12, 2008. Accepted May 15, 2008.

The eukaryotic RecA homologs Rad51 and Dmc1 are essential for strand exchange between homologous chromosomes during meiosis. All members of the RecA family of recombinases polymerize on DNA to form helical nucleoprotein filaments, which is the active form of the protein. Here we compare the filament structures of the Rad51 and Dmc1 proteins from both human and budding yeast. Previous studies of Dmc1 filaments suggested that they might be structurally distinct from filaments of other members of the RecA family, including Rad51. The data presented here indicate that Rad51 and Dmc1 filaments are essentially identical with respect to several structural parameters, including persistence length, helical pitch, filament diameter, DNA base pairs per helical turn and helical handedness. These data, together with previous studies demonstrating similar in vitro recombinase activity for Dmc1 and Rad51, support the view that differences in the meiotic function of Rad51 and Dmc1 are more likely to result from the influence of distinct sets of accessory proteins than from intrinsic differences in filament structure.


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