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

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.
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
Science
Date: Oct. 24, 2008
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