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Nucleic Acids Research Advance Access originally published online on January 16, 2009
Nucleic Acids Research 2009 37(5):1580-1588; doi:10.1093/nar/gkn1072
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Nucleic Acids Research, 2009, Vol. 37, No. 5 1580-1588
© 2009 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

RAD50 and NBS1 form a stable complex functional in DNA binding and tethering

Eddy van der Linden1, Humberto Sanchez1, Eri Kinoshita1, Roland Kanaar1,2 and Claire Wyman1,2,*

1Department of Cell Biology and Genetics, Cancer Genomics Center and 2Department of Radiation Oncology, Erasmus MC, PO Box 2040, 3000 CA Rotterdam, The Netherlands

*To whom correspondence should be addressed. Tel: +31 10 704 4337; Fax: +31 10 704 4743; Email: c.wyman{at}erasmusmc.nl

Received November 28, 2008. Revised December 19, 2008. Accepted December 22, 2008.

The RAD50/MRE11/NBS1 protein complex (RMN) plays an essential role during the early steps of DNA double-strand break (DSB) repair by homologous recombination. Previous data suggest that one important role for RMN in DSB repair is to provide a link between DNA ends. The striking architecture of the complex, a globular domain from which two extended coiled coils protrude, is essential for this function. Due to its DNA-binding activity, ability to form dimers and interact with both RAD50 and NBS1, MRE11 is considered to be crucial for formation and function of RMN. Here, we show the successful expression and purification of a stable complex containing only RAD50 and NBS1 (RN). The characteristic architecture of the complex was not affected by absence of MRE11. Although MRE11 is a DNA-binding protein it was not required for DNA binding per se or DNA-tethering activity of the complex. The stoichiometry of NBS1 in RMN and RN complexes was estimated by SFM-based volume analysis. These data show that in vitro, R, M and N form a variety of stable complexes with variable subunit composition and stoichiometry, which may be physiologically relevant in different aspects of RMN function.


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