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

Molecular cell | Feb 10, 2012

http://www.ncbi.nlm.nih.gov/pubmed/22285753

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 RIS Download

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

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Associated grants

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

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