Proteome mapping of the Trichoderma reesei 20S proteasome
Proteome mapping of the Trichoderma reesei 20S proteasome
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DOI：
10.1007/s00294-006-0108-8
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发表时间：
2007-02-01
期刊：
影响因子：
2.5
通讯作者：
Nevalainen, Helena
中科院分区：
文献类型：
--
作者：
Grinyer, Jasmine;Kautto, Liisa;Nevalainen, Helena
26S蛋白酶体是一种由催化20S核心颗粒和19S调节颗粒组成的多催化蛋白水解酶，在细胞蛋白质质量控制中起着至关重要的作用。我们使用基于层析的方法从工业化开发的丝状真菌里氏木霉中纯化并定位了20S核心颗粒的蛋白质含量。目前还没有关于丝状真菌蛋白酶体的分离或蛋白质组学图谱的报道。从参考图谱中，已经鉴定了14个20S蛋白酶体亚基中的13个以及与20S蛋白酶体共纯化的许多相关蛋白。这些蛋白包括78 kDa葡萄糖调节蛋白(BIP)和几个伴侣蛋白，包括参与未折叠蛋白反应(UPR)的热休克蛋白。蛋白质组图谱上还发现了一些蛋白酶体相互作用蛋白(PIP)，包括14-3-3-样蛋白、甘油醛-3-磷酸脱氢酶、转醛酶、肌动蛋白、翻译延伸因子、烯醇酶、内质网中的ATPase(CDC48)和真核启动因子。我们在这里提供了20S催化核心的主图，为未来丝状真菌内源和外源蛋白在细胞内降解的差异显示研究铺平了道路。
The 26S proteasome, a multicatalytic protease comprising the catalytic 20S core particle and the 19S regulatory particle has a crucial role in cellular protein quality control. We have used a chromatography-based approach to purify and map the protein content of the 20S core particle from the industrially-exploited filamentous fungus Trichoderma reesei. There are no previous reports on the isolation or proteomic mapping of the proteasome from any filamentous fungus. From the reference map, 13 of the 14 20S proteasome subunits and many related proteins that co-purified with the 20S proteasome have been identified. These include 78 kDa glucose-regulated protein (BIP) and several chaperones including heat shock proteins involved in the unfolded protein response (UPR). Some proteasome interacting proteins (PIPs) were also identified on the proteome map and included 14-3-3-like protein, glyceraldehyde-3-phosphate dehydrogenase, transaldolase, actin, translation elongation factor, enolase, ATPase in the ER (CDC48), and eukaryotic initiation factor. We present here a master map for the 20S catalytic core to pave the way for future differential display studies addressing intracellular degradation of endogenous and foreign proteins in filamentous fungi.