Yeast Xrs2 Binds DNA and Helps Target Rad50 and Mre11 to DNA Ends

Saccharomyces cerevisiae Rad50, Mre11, and Xrs2 proteins are involved in homologous recombination, non-homologous end-joining, DNA damage checkpoint signaling, and telomere maintenance. These proteins form a stable complex that has nuclease, DNA binding, and DNA end recognition activities. Of the co...

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Bibliographic Details
Published in:The Journal of biological chemistry 2003-12, Vol.278 (49), p.48957-48964
Main Authors: Trujillo, Kelly M., Roh, Dong Hyun, Chen, Ling, Van Komen, Stephen, Tomkinson, Alan, Sung, Patrick
Format: Article
Language:English
Subjects:
Adenosine Triphosphatases - metabolism
Base Sequence
DNA Helicases
DNA, Fungal - metabolism
DNA-Binding Proteins - metabolism
Endodeoxyribonucleases - metabolism
Exodeoxyribonucleases - metabolism
Mre11 protein
Rad50 protein
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - isolation & purification
Saccharomyces cerevisiae Proteins - metabolism
Xrs2 protein
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Summary:Saccharomyces cerevisiae Rad50, Mre11, and Xrs2 proteins are involved in homologous recombination, non-homologous end-joining, DNA damage checkpoint signaling, and telomere maintenance. These proteins form a stable complex that has nuclease, DNA binding, and DNA end recognition activities. Of the components of the Rad50·Mre11·Xrs2 complex, Xrs2 is the least characterized. The available evidence is consistent with the idea that Xrs2 recruits other protein factors in reactions that pertain to the biological functions of the Rad50·Mre11·Xrs2 complex. Here we present biochemical evidence that Xrs2 has an associated DNA-binding activity that is specific for DNA structures. We also define the contributions of Xrs2 to the activities of the Rad50·Mre11·Xrs2 complex. Importantly, we demonstrate that Xrs2 is critical for targeting of Rad50 and Mre11 to DNA ends. Thus, Xrs2 likely plays a direct role in the engagement of DNA substrates by the Rad50· Mre11·Xrs2 complex in various biological processes.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M309877200