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Molecular and Cellular Biology, November 1999, p. 7681-7687, Vol. 19, No. 11
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The Mre11-Rad50-Xrs2 Protein Complex Facilitates Homologous Recombination-Based Double-Strand Break Repair in Saccharomyces cerevisiaedagger

Debra A. Bressan, Bonnie K. Baxter, and John H. J. Petrini*

Laboratory of Genetics, University of Wisconsin Medical School, Madison, Wisconsin 53706

Received 16 June 1999/Returned for modification 30 July 1999/Accepted 19 August 1999

Saccharomyces cerevisiae mre11Delta mutants are profoundly deficient in double-strand break (DSB) repair, indicating that the Mre11-Rad50-Xrs2 protein complex plays a central role in the cellular response to DNA DSBs. In this study, we examined the role of the complex in homologous recombination, the primary mode of DSB repair in yeast. We measured survival in synchronous cultures following irradiation and scored sister chromatid and interhomologue recombination genetically. mre11Delta strains were profoundly sensitive to ionizing radiation (IR) throughout the cell cycle. Mutant strains exhibited decreased frequencies of IR-induced sister chromatid and interhomologue recombination, indicating a general deficiency in homologous recombination-based DSB repair. Since a nuclease-deficient mre11 mutant was not impaired in these assays, it appears that the role of the S. cerevisiae Mre11-Rad50-Xrs2 protein complex in facilitating homologous recombination is independent of its nuclease activities.


* Corresponding author. Mailing address: Laboratory of Genetics, University of Wisconsin Medical School, 445 Henry Mall, Madison, WI 53706. Phone: (608) 265-6043. Fax: (608) 262-2976. E-mail: jpetrini{at}facstaff.wisc.edu.

dagger Manuscript 3538 from the University of Wisconsin---Madison Laboratory of Genetics.


Molecular and Cellular Biology, November 1999, p. 7681-7687, Vol. 19, No. 11
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



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