Regulating global sumoylation by a MAP kinase Hog1 and its potential role in osmo-tolerance in yeast.
Regulating global sumoylation by a MAP kinase Hog1 and its potential role in osmo-tolerance in yeast.
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DOI：
10.1371/journal.pone.0087306
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发表时间：
2014
期刊：
影响因子：
3.7
通讯作者：
Wang Y
中科院分区：
文献类型：
--
作者：
Abu Irqeba A;Li Y;Panahi M;Zhu M;Wang Y
SUMO化是一种由小泛素样修饰物（SUMO）引起的蛋白质翻译后修饰，参与了许多应激反应。在这里，我们分析了sumoylation在酵母中的抑制反应中的潜在作用。我们发现，渗透胁迫诱导sumoylated物种在正常酵母细胞中的快速积累。有趣的是，MAP激酶Hog1的破坏导致更高水平的sumoylated共轭物的积累，这是独立的新蛋白质的合成。我们还发现，sumoylated物种的积累是依赖于SUMO连接酶Siz1。值得注意的是，在HOG1破坏突变体（hog1Δ）中而不是在野生型细胞中SIZ1的过表达导致sumoylated物质的显著增加和延长的积累。检查酵母突变体的耐盐性，显示无论是增加或减少的整体sumoylation水平，揭示了sumoylated共轭物和耐盐性的积累之间的反比关系。进一步的研究表明，许多由高渗胁迫诱导的sumoylated物质实际上是聚sumoylated。总之，这些研究结果表明，异常积累的多sumoylated共轭物是有害的酵母菌的耐盐性，并建议Hog1促进适应高渗胁迫部分通过调节全球sumoylation水平。
Sumoylation, a post-translational protein modification by small ubiquitin-like modifier (SUMO), has been implicated in many stress responses. Here we analyzed the potential role of sumoylation in osmo-response in yeast. We find that osmotic stress induces rapid accumulation of sumoylated species in normal yeast cells. Interestingly, disruption of MAP kinase Hog1 leads to a much higher level of accumulation of sumoylated conjugates that are independent of new protein synthesis. We also find that the accumulation of sumoylated species is dependent on a SUMO ligase Siz1. Notably, overexpression of SIZ1 in HOG1-disruption mutants (hog1Δ) but not in wild type cells leads to a markedly increased and prolonged accumulation of sumoylated species. Examination of osmo-tolerance of yeast mutants that display either an increase or a decrease in the global sumoylation level revealed an inverse relationship between accumulation of sumoylated conjugates and osmo-tolerance. Further investigation has shown that many of the sumoylated species induced by hyperosmotic stress are actually poly-sumoylated. Together, these findings indicate that abnormal accumulation of poly-sumoylated conjugates is harmful for osmo-tolerance in yeast, and suggest that Hog1 promotes adaptation to hyperosmotic stress partially via regulation of global sumoylation level.
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