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Formation of the yeast Mre11-Rad50-Xrs2 complex is correlated with DNA repair and telomere maintenance.
Nucleic Acids Res. 1999 May 15; 27(10):2072-9.NA

Abstract

The yeast Mre11 is a multi-functional protein and is known to form a protein complex with Rad50 and Xrs2. In order to elucidate the relationship between Mre11 complex formation and its mitotic functions, and to determine domain(s) required for Mre11 protein interactions, we performed yeast two-hybrid and functional analyses with respect to Mre11 DNA repair and telomere maintenance. Evidence presented in this study indicates that the N-terminal region of Mre11 constitutes the core homo-dimerization and hetero-dimerization domain and is sufficient for Mre11 DNA repair and maintaining the wild-type telomere length. In contrast, a stretch of 134 amino acids from the extreme C-terminus, although essential for achieving a full level of self-association, is not required for the aforementioned Mre11 mitotic functions. Interestingly, deletion of these same 134 amino acids enhanced the interaction of Mre11 with Rad50 and Xrs2, which is consistent with the notion that this region is specific for meiotic functions. While Mre11 self-association alone is insufficient to provide the above mitotic activities, our results are consistent with a strong correlation between Mre11-Rad50-Xrs2 complex formation, mitotic DNA repair and telomere maintenance. This correlation was further strengthened by analyzing two mre11 phosphoesterase motif mutants (mre11-2 and rad58S), which are defective in DNA repair, telomere maintenance and protein interactions, and a rad50S mutant, which is normal in both complex formation and mitotic functions. Together, these results support and extend a current model regarding Mre11 structure and functions in mitosis and meiosis.

Authors+Show Affiliations

Department of Microbiology and Immunology, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK S7N 5E5, Canada.No affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

10219078

Citation

Chamankhah, M, and W Xiao. "Formation of the Yeast Mre11-Rad50-Xrs2 Complex Is Correlated With DNA Repair and Telomere Maintenance." Nucleic Acids Research, vol. 27, no. 10, 1999, pp. 2072-9.
Chamankhah M, Xiao W. Formation of the yeast Mre11-Rad50-Xrs2 complex is correlated with DNA repair and telomere maintenance. Nucleic Acids Res. 1999;27(10):2072-9.
Chamankhah, M., & Xiao, W. (1999). Formation of the yeast Mre11-Rad50-Xrs2 complex is correlated with DNA repair and telomere maintenance. Nucleic Acids Research, 27(10), 2072-9.
Chamankhah M, Xiao W. Formation of the Yeast Mre11-Rad50-Xrs2 Complex Is Correlated With DNA Repair and Telomere Maintenance. Nucleic Acids Res. 1999 May 15;27(10):2072-9. PubMed PMID: 10219078.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Formation of the yeast Mre11-Rad50-Xrs2 complex is correlated with DNA repair and telomere maintenance. AU - Chamankhah,M, AU - Xiao,W, PY - 1999/4/29/pubmed PY - 1999/4/29/medline PY - 1999/4/29/entrez SP - 2072 EP - 9 JF - Nucleic acids research JO - Nucleic Acids Res VL - 27 IS - 10 N2 - The yeast Mre11 is a multi-functional protein and is known to form a protein complex with Rad50 and Xrs2. In order to elucidate the relationship between Mre11 complex formation and its mitotic functions, and to determine domain(s) required for Mre11 protein interactions, we performed yeast two-hybrid and functional analyses with respect to Mre11 DNA repair and telomere maintenance. Evidence presented in this study indicates that the N-terminal region of Mre11 constitutes the core homo-dimerization and hetero-dimerization domain and is sufficient for Mre11 DNA repair and maintaining the wild-type telomere length. In contrast, a stretch of 134 amino acids from the extreme C-terminus, although essential for achieving a full level of self-association, is not required for the aforementioned Mre11 mitotic functions. Interestingly, deletion of these same 134 amino acids enhanced the interaction of Mre11 with Rad50 and Xrs2, which is consistent with the notion that this region is specific for meiotic functions. While Mre11 self-association alone is insufficient to provide the above mitotic activities, our results are consistent with a strong correlation between Mre11-Rad50-Xrs2 complex formation, mitotic DNA repair and telomere maintenance. This correlation was further strengthened by analyzing two mre11 phosphoesterase motif mutants (mre11-2 and rad58S), which are defective in DNA repair, telomere maintenance and protein interactions, and a rad50S mutant, which is normal in both complex formation and mitotic functions. Together, these results support and extend a current model regarding Mre11 structure and functions in mitosis and meiosis. SN - 0305-1048 UR - https://www.unboundmedicine.com/medline/citation/10219078/Formation_of_the_yeast_Mre11_Rad50_Xrs2_complex_is_correlated_with_DNA_repair_and_telomere_maintenance_ DB - PRIME DP - Unbound Medicine ER -