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Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase.

Science (New York, N.Y.) | Oct 24, 2008

http://www.ncbi.nlm.nih.gov/pubmed/18948542

Recent findings suggest important roles for nuclear organization in gene expression. In contrast, little is known about how nuclear organization contributes to genome stability. Epistasis analysis (E-MAP) using DNA repair factors in yeast indicated a functional relationship between a nuclear pore subcomplex and Slx5/Slx8, a small ubiquitin-like modifier (SUMO)-dependent ubiquitin ligase, which we show physically interact. Real-time imaging and chromatin immunoprecipitation confirmed stable recruitment of damaged DNA to nuclear pores. Relocation required the Nup84 complex and Mec1/Tel1 kinases. Spontaneous gene conversion can be enhanced in a Slx8- and Nup84-dependent manner by tethering donor sites at the nuclear periphery. This suggests that strand breaks are shunted to nuclear pores for a repair pathway controlled by a conserved SUMO-dependent E3 ligase.

Pubmed ID: 18948542 RIS Download

Mesh terms: Chromatin Immunoprecipitation | DNA Breaks, Double-Stranded | DNA Repair | DNA, Fungal | DNA-Binding Proteins | Deoxyribonucleases, Type II Site-Specific | Gene Conversion | Genes, Fungal | Immunoprecipitation | Intracellular Signaling Peptides and Proteins | Kinetics | Nuclear Pore | Nuclear Pore Complex Proteins | Protein-Serine-Threonine Kinases | Recombination, Genetic | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Small Ubiquitin-Related Modifier Proteins | Ubiquitin-Protein Ligases | Zinc Fingers

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM084448

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