Physical and Genetic Interactions Between Uls1 and the Slx5-Slx8 SUMO-Targeted Ubiquitin Ligase.
Physical and Genetic Interactions Between Uls1 and the Slx5-Slx8 SUMO-Targeted Ubiquitin Ligase.
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DOI：
10.1534/g3.113.005827
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发表时间：
2013-04-09
期刊：
影响因子：
--
通讯作者：
Prelich G
中科院分区：
文献类型：
--
作者：
Tan W;Wang Z;Prelich G
Slx5-Slx8复合物是一种泛素连接酶，它优先泛素化SUMOylated底物，靶向它们进行蛋白质水解。SLX5、SLX8和其他SUMO通路基因的突变先前在我们的实验室中被鉴定为转录调节因子MOT1中点突变（MOT1 -301）的基因组抑制因子。为了进一步了解SUMO和泛素通路之间的联系，对mot1-301的高拷贝抑制基因进行了筛选，得到了三个基因（MOT3， MIT1和ULS1）。MOT3和MIT1具有朊病毒的特征，ULS1被认为编码另一种sumo靶向的泛素连接酶（STUbL），其功能与Slx5-Slx8重叠。这里我们关注ULS1，得到的结果表明ULS1和SLX5之间的关系比预期的要复杂。在酵母双杂交和共免疫沉淀实验中，Uls1与Slx5发生物理相互作用，Uls1突变阻断了Uls1与Slx5的相互作用，干扰了Uls1的功能，遗传学分析表明Uls1与Slx5之间存在拮抗关系。综上所述，我们的研究结果挑战了Uls1和Slx5只是部分重叠的STUbLs的假设，并开始阐明这两种蛋白之间的调节关系。
The Slx5–Slx8 complex is a ubiquitin ligase that preferentially ubiquitylates SUMOylated substrates, targeting them for proteolysis. Mutations in SLX5, SLX8, and other SUMO pathway genes were previously identified in our laboratory as genomic suppressors of a point mutation (mot1-301) in the transcriptional regulator MOT1. To further understand the links between the SUMO and ubiquitin pathways, a screen was performed for high-copy suppressors of mot1-301, yielding three genes (MOT3, MIT1, and ULS1). MOT3 and MIT1 have characteristics of prions, and ULS1 is believed to encode another SUMO-targeted ubiquitin ligase (STUbL) that functionally overlaps with Slx5-Slx8. Here we focus on ULS1, obtaining results suggesting that the relationship between ULS1 and SLX5 is more complex than expected. Uls1 interacted with Slx5 physically in to yeast two-hybrid and co-immunoprecipitation assays, a uls1 mutation that blocked the interaction between Uls1 and Slx5 interfered with ULS1 function, and genetic analyses indicated an antagonistic relationship between ULS1 and SLX5. Combined, our results challenge the assumption that Uls1 and Slx5 are simply partially overlapping STUbLs and begin to illuminate a regulatory relationship between these two proteins.
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