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

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  • 2008-10-25
Published in:
  • Science (New York, N.Y.). - 2008
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
English 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.
Language
  • English
Open access status
green
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Persistent URL
https://sonar.ch/global/documents/129706
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