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Cyclin-dependent kinase modulates budding yeast Rad5 stability during cell cycle.

Masafumi Hayashi1, Kenji Keyamura1, Takashi Hishida1

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Cyclin-dependent kinase 1 (CDK1) controls the stability of the Rad5 protein by phosphorylation during the cell cycle. This regulation is crucial for proper DNA damage tolerance and cell cycle progression.

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Area of Science:

  • Molecular Biology
  • Cell Cycle Regulation
  • DNA Repair

Background:

  • The DNA damage tolerance (DDT) pathway is essential for bypassing DNA lesions during replication.
  • Rad5 protein in Saccharomyces cerevisiae is key to the error-free DDT pathway and its levels fluctuate cyclically.
  • The precise mechanisms and functional significance of Rad5's cell cycle regulation are not fully understood.

Purpose of the Study:

  • To investigate the regulation of Rad5 protein levels during the cell cycle.
  • To determine the role of phosphorylation in Rad5 stability and function.
  • To elucidate the interplay between Rad5 phosphorylation, degradation, and cell cycle control.

Main Methods:

  • Phosphorylation site mapping of Rad5.
  • Analysis of Rad5 protein half-life in wild-type and mutant cells.
  • Cell cycle analysis of Rad5 phosphorylation and stability.
  • Investigating the role of cyclin-dependent kinase Cdc28/CDK1.

Main Results:

  • Rad5 is phosphorylated on serine 130 (S130) during S/G2 phase, dependent on Cdc28/CDK1.
  • Phosphorylated Rad5 (S130) has a shorter half-life than non-phosphorylated Rad5.
  • Cells with a phosphorylation-defective S130A mutation show partially stabilized Rad5 protein.
  • Eliminating S130 phosphorylation disrupts the cell-cycle-dependent oscillation of Rad5 levels.

Conclusions:

  • CDK1-mediated phosphorylation of Rad5 at S130 regulates its protein stability during the cell cycle.
  • This phosphorylation-degradation crosstalk is critical for maintaining Rad5's cell cycle oscillation.
  • The findings provide insight into the coordinated regulation of DNA damage tolerance and cell cycle progression.