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Vol. 16, Issue 2, 597-608, February 2005

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Xrs2p Regulates Mre11p Translocation to the Nucleus and Plays a Role in Telomere Elongation and Meiotic Recombination

Iwate College of Nursing, Iwate 020-0151, Japan

Submitted September 7, 2004; Revised October 13, 2004; Accepted October 28, 2004
Monitoring Editor: Douglas Koshland

The Mre11-Rad50-Xrs2 (MRX) protein complex plays pivotal roles in meiotic recombination, repair of damaged DNA, telomere elongation, and cell cycle checkpoint control. Xrs2p is known to be essential for all the functions of the complex, but its role in the complex has not been clearly elucidated. A 32-amino acid region near the C terminus of Xrs2p was identified as an Mre11p-binding site. No more function of Xrs2p than translocation of Mre11p from the cytoplasm to the nucleus is necessary for response to DNA damage. However, domains in Xrs2p located both 49 amino acids upstream and 104 amino acids downstream of the Mre11p binding site are required for meiotic recombination and telomere elongation, respectively, in addition to the 32-amino acid region. These findings demonstrate that Xrs2p acts as a specificity factor that allows the MRX complex to function in meiotic recombination and in telomere elongation.

The online version of this article contains supplemental material at MBC Online (http://www.molbiolcell.org).

^* Corresponding author. E-mail address: tsukamot{at}iwate-nurse.ac.jp.

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