Nucleic Acids Research, 2003, Vol. 31, No. 6 1715-1724
© 2003 Oxford University Press
The ATM-related Tel1 protein of Saccharomyces cerevisiae controls a checkpoint response following phleomycin treatment
Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-0814, Japan
*To whom correspondence should be addressed. Tel: +81 52 789 2593; Fax: +81 52 789 2589; Email: j46036a{at}nucc.cc.nagoya-u.acjp
Present address:
Toshiyasu Shimomura, Tsukuba Research Institute, Banyu Pharmaceutical Co., Ltd, Tsukuba 300-2611, Japan
MEC1 and TEL1 encode ATR- and ATM-related proteins in the budding yeast Saccharomyces cerevisiae, respectively. Phleomycin is an agent that catalyzes double-strand breaks in DNA. We show here that both Mec1 and Tel1 regulate the checkpoint response following phleomycin treatment. MEC1 is required for Rad53 phosphorylation and cell-cycle progression delay following phleomycin treatment in G1, S or G2/M phases. The tel1
mutation confers a defect in the checkpoint responses to phleomycin treatment in S phase. In addition, the tel1 mutation enhances the mec1 defect in activation of the phleomycin-induced checkpoint pathway in S phase. In contrast, the tel1 mutation confers only a minor defect in the checkpoint responses in G1 phase and no apparent defect in G2/M phase. Methyl methanesulfonate (MMS) treatment also activates checkpoints, inducing Rad53 phosphorylation in S phase. MMS-induced Rad53 phosphorylation is not detected in mec1 mutants during S phase, but occurs in tel1 mutants similar to wild-type cells. Finally, Xrs2 is phosphorylated after phleomycin treatment in a TEL1-dependent manner during S phase, whereas no significant Xrs2 phosphorylation is detected after MMS treatment. Together, our results support a model in which Tel1 contributes to checkpoint control in response to phleomycin-induced DNA damage in S phase.
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