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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.

Pubmed ID: 18948542

Authors

  • Nagai S
  • Dubrana K
  • Tsai-Pflugfelder M
  • Davidson MB
  • Roberts TM
  • Brown GW
  • Varela E
  • Hediger F
  • Gasser SM
  • Krogan NJ

Journal

Science (New York, N.Y.)

Publication Data

October 24, 2008

Associated Grants

  • Agency: NIGMS NIH HHS, Id: R01 GM084448

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