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Extensive DNA damage-induced sumoylation contributes to replication and repair and acts in addition to the mec1 checkpoint.

The cellular response to DNA damage employs multiple dynamic protein modifications to exert rapid and adaptable effects. Substantial work has detailed the roles of canonical checkpoint-mediated phosphorylation in this program. Recent studies have also implicated sumoylation in the DNA damage response; however, a systematic view of the contribution of sumoylation to replication and repair and its interplay with checkpoints is lacking. Here, using a biochemical screen in yeast, we establish that DNA damage-induced sumoylation occurs on a large scale. We identify MRX (Mre11-Rad50-Xrs2) as a positive regulator of this induction for a subset of repair targets. In addition, we find that defective sumoylation results in failure to complete replication of a damaged genome and impaired DNA end processing, highlighting the importance of the SUMO-mediated response in genome integrity. We also show that DNA damage-induced sumoylation does not require Mec1 checkpoint signaling, and the presence of both enables optimal DNA damage resistance.

Pubmed ID: 22285753


  • Cremona CA
  • Sarangi P
  • Yang Y
  • Hang LE
  • Rahman S
  • Zhao X


Molecular cell

Publication Data

February 10, 2012

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM080670
  • Agency: NIGMS NIH HHS, Id: R01 GM080670-04
  • Agency: NIGMS NIH HHS, Id: R01GM080670

Mesh Terms

  • Cell Cycle Checkpoints
  • DNA Damage
  • DNA Repair
  • DNA Repair Enzymes
  • DNA Replication
  • DNA-Binding Proteins
  • Gene Knockout Techniques
  • Genome, Fungal
  • Genomic Instability
  • Intracellular Signaling Peptides and Proteins
  • Microbial Viability
  • Multiprotein Complexes
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protein-Serine-Threonine Kinases
  • Saccharomyces cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Sumoylation