Functional targeting of DNA damage to a nuclear pore-associated SUMO-dependent ubiquitin ligase.
作者： S. Nagai , K. Dubrana , M. Tsai-Pflugfelder , M. B. Davidson , T. M. Roberts
关键词: DNA repair 、 Chromatin immunoprecipitation 、 Biochemistry 、 Nuclear pore 、 DNA damage 、 Biology 、 Gene expression 、 Small Ubiquitin-Related Modifier Proteins 、 Cell biology 、 Ubiquitin ligase 、 Immunoprecipitation
摘要: Recent findings suggest important roles for nuclear organization in gene expression. In contrast, little is known about how contributes to genome stability. Epistasis analysis (E-MAP) using DNA repair factors yeast indicated a functional relationship between pore subcomplex and Slx5/Slx8, small ubiquitin-like modifier (SUMO)–dependent ubiquitin ligase, which we show physically interact. Real-time imaging chromatin immunoprecipitation confirmed stable recruitment of damaged pores. Relocation required the Nup84 complex Mec1/Tel1 kinases. Spontaneous conversion can be enhanced Slx8- Nup84-dependent manner by tethering donor sites at periphery. This suggests that strand breaks are shunted pores pathway controlled conserved SUMO-dependent E3 ligase.
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