Nucleic Acids Research, Vol 27, Issue 10 2072-2079, Copyright © 1999 by Oxford University Press
M Chamankhah and W Xiao
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.
ARTICLES
Formation of the yeast Mre11-Rad50-Xrs2 complex is correlated with DNA repair and telomere maintenance
Department of Microbiology and Immunology, University of Saskatchewan, 107 Wiggins Road, Saskatoon, SK S7N 5E5, Canada.
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