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To misfold or to lose structure?: Detection and degradation of oxidized proteins by the 20S proteasome

机译：要折叠还是丢失结构？：20S蛋白酶体检测并降解氧化的蛋白质

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摘要

Aggregation of proteins damaged by stress is often a causal factor of cell death. To prevent aggregation, eukaryotic cells rapidly degrade damaged proteins by engaging two types of proteasomes. The first type is the 26S proteasome (26SP) which is composed of a cylindrical proteolytic core—the 20S proteasome (20SP)—and one or two regulatory particles (RPs) that interact with ubiquitinated proteins. The second type is the free 20SP which mediates ubiquitin-independent proteolysis. We have recently shown that loss of RP function in Arabidopsis leads to an expected decrease in 26SP-dependent protein degradation and hypersensitivity to stresses that induce protein misfolding. Surprisingly, RP mutants have increased 20SP activity and tolerance to oxidative stress. This finding suggests that misfolded proteins carry one type of degradation signal that steers them to ubiquitination enzymes and the 26SP, while oxidatively damaged proteins carry another that guides them directly to the 20SP for degradation. Here we suggest that protein oxidation induces the formation of unstructured regions that serve as targeting signals for 20SP-dependent proteolysis.
机译：受压力破坏的蛋白质聚集通常是细胞死亡的原因。为了防止聚集，真核细胞通过结合两种蛋白酶体来迅速降解受损的蛋白质。第一种是26S蛋白酶体（26SP），它由圆柱形的蛋白水解核心-20S蛋白酶体（20SP）-和一个或两个与泛素化蛋白质相互作用的调节颗粒（RP）组成。第二种是游离的20SP，它介导不依赖泛素的蛋白水解。我们最近显示，拟南芥中RP功能的丧失导致预期的26SP依赖性蛋白降解降低以及对诱导蛋白错误折叠的应激超敏。令人惊讶的是，RP突变体具有增加的20SP活性和对氧化应激的耐受性。这一发现表明，折叠错误的蛋白质会携带一种降解信号，将其引导至泛素化酶和26SP，而氧化受损的蛋白质则会携带另一种信号，将其直接引导至20SP进行降解。在这里，我们建议蛋白质氧化诱导非结构化区域的形成，该区域用作20SP依赖性蛋白水解的靶向信号。

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