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Originally published In Press as doi:10.1074/jbc.M106179200 on July 24, 2001

J. Biol. Chem., Vol. 276, Issue 40, 37027-37033, October 5, 2001
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Structure of the Rad50·Mre11 DNA Repair Complex from Saccharomyces cerevisiae by Electron Microscopy*

David E. AndersonDagger , Kelly M. Trujillo§, Patrick Sung§, and Harold P. EricksonDagger

From the Dagger  Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710-3709 and the § Department of Molecular Medicine and Institute of Biotechnology, University of Texas Health Science Center at San Antonio, San Antonio, Texas, 78245-3207

The RAD50 gene of Saccharomyces cerevisiae is one of several genes required for recombinational repair of double-strand DNA breaks during vegetative growth and for initiation of meiotic recombination. Rad50 forms a complex with two other proteins, Mre11 and Xrs2, and this complex is involved in double-strand break formation and processing. Rad50 has limited sequence homology to the structural maintenance of chromosomes (SMC) family of proteins and shares the same domain structure as SMCs: N- and C-terminal globular domains separated by two long coiled-coils. However, a notable difference is the much smaller non-coil hinge region between the two coiled-coils. We report here a structural analysis of full-length S. cerevisiae Rad50, alone and in a complex with yeast Mre11 by electron microscopy. Our results confirm that yeast Rad50 does have the same antiparallel coiled-coil structure as SMC proteins, but with no detectable globular hinge domain. However, the molecule is still able to bend sharply in the middle to bring the two catalytic domains together, indicating that the small hinge domain is flexible. We also demonstrate that Mre11 binds as a dimer between the catalytic domains of Rad50, bringing the nuclease activities of Mre11 in close proximity to the ATPase and DNA binding activities of Rad50.

* This work was supported by National Institutes of Health Grants GM28553, ES07061, GM57814, and CA81020 and by Human Frontier Science Project Grant RG0178/2000-M.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

To whom correspondence should be addressed: Department of Cell Biology, Box 3709, Duke University Medical Center, Durham, NC 27710. E-mail: H.Erickson@cellbio.duke.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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