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Visualizing and Quantifying Endonuclease-Based Site-Specific DNA Damage
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Sequential primed kinases create a damage-responsive phosphodegron on Eco1.

Nicholas A Lyons1, Bryan R Fonslow, Jolene K Diedrich

  • 1Department of Physiology, University of California, San Francisco, San Francisco, California, USA.

Nature Structural & Molecular Biology
|January 15, 2013
PubMed
Summary
This summary is machine-generated.

Sister-chromatid cohesion relies on Eco1 acetylation. Three kinases sequentially phosphorylate Eco1, enabling its degradation and controlling cohesion establishment during cell growth and stress.

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Area of Science:

  • Cell Biology
  • Molecular Biology
  • Genetics

Background:

  • Sister-chromatid cohesion is crucial for accurate chromosome segregation during cell division.
  • Eco1 acetylates cohesin to establish this cohesion during S phase.
  • Eco1 activity is tightly regulated post-S phase through phosphorylation and ubiquitination.

Purpose of the Study:

  • To elucidate the sequential kinase-dependent regulation of Eco1 degradation.
  • To understand how Eco1 destruction is precisely controlled after S phase.
  • To investigate the role of DNA damage response in regulating Eco1 stability.

Main Methods:

  • Budding yeast as a model organism.
  • Analysis of Eco1 phosphorylation and ubiquitination.
  • Inhibition of specific kinases (Cdk1, Cdc7-Dbf4, Mck1) and ubiquitin ligase (SCF(Cdc4)).

Main Results:

  • Eco1 degradation requires sequential phosphorylation by Cdk1, Cdc7-Dbf4, and Mck1.
  • Cdc7-Dbf4 and Mck1 phosphorylation create specific docking sites for SCF(Cdc4).
  • DNA damage response-mediated inhibition of Cdc7 prevents Eco1 destruction, allowing post-S phase cohesion.

Conclusions:

  • A multi-kinase cascade ensures ordered Eco1 phosphorylation and degradation.
  • SCF(Cdc4) exhibits strict substrate discrimination based on phosphorylation patterns.
  • This regulatory system provides robust control of cohesion establishment in response to cell cycle progression and stress.