Preparing your results

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

The ATM-related Tel1 protein of Saccharomyces cerevisiae controls a checkpoint response following phleomycin treatment.

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 tel1Delta mutation confers a defect in the checkpoint responses to phleomycin treatment in S phase. In addition, the tel1Delta mutation enhances the mec1 defect in activation of the phleomycin-induced checkpoint pathway in S phase. In contrast, the tel1Delta 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 mec1Delta mutants during S phase, but occurs in tel1Delta 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.

Pubmed ID: 12626713


  • Nakada D
  • Shimomura T
  • Matsumoto K
  • Sugimoto K


Nucleic acids research

Publication Data

March 15, 2003

Associated Grants


Mesh Terms

  • Cell Cycle
  • Cell Cycle Proteins
  • Checkpoint Kinase 2
  • Fungal Proteins
  • G2 Phase
  • Intracellular Signaling Peptides and Proteins
  • Methyl Methanesulfonate
  • Mitosis
  • Mutation
  • Nucleic Acid Synthesis Inhibitors
  • Phleomycins
  • Phosphorylation
  • Protein-Serine-Threonine Kinases
  • S Phase
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins