Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae
Dissection of the assembly pathway of the proteasome lid in Saccharomyces cerevisiae
复制标题
DOI：
10.1016/j.bbrc.2010.05.061
复制
发表时间：
2010-06-11
影响因子：
3.1
通讯作者：
Saeki, Yasushi
中科院分区：
文献类型：
--
作者：
Fukunaga, Keisuke;Kudo, Tai;Saeki, Yasushi
26S蛋白酶体是一种高度保守的多亚基蛋白酶，在真核细胞中降解泛素化蛋白。它包括一个20S核心颗粒和两个19S调节颗粒，其进一步分为盖状复合物和底状复合物。lid是一个9亚基复合物，在结构上与COP9信号体和真核起始因子3相关。虽然20S和基部的组装途径已经被很好地描述，但是盖子的组装途径仍然不清楚。在这项研究中，我们使用酵母盖子突变细胞rpn7-3、Delta rpn9和rpn12-1解剖了盖子组装。通过质谱分析，我们在突变体中发现了许多盖子亚组件，如Rpn3-Rpn7对和缺乏Rpn12的盖子状复合体。我们的分析表明，盖子的组装是一个高度有序和多步骤的过程；首先，将Rpn5、6、8、9、11组装成核心模块，然后连接由Rpn3、7、Semi组成的第二模块，随后将Rpn12并入形成盖子配合物。(C) 2010爱思唯尔公司版权所有。
The 26S proteasome is a highly conserved multisubunit protease that degrades ubiquitinated proteins in eukaryotic cells. It comprises a 20S core particle and two 19S regulatory particles that are further divided into the lid and base complexes. The lid is a nine subunits complex that is structurally related to the COP9 signalosome and the eukaryotic initiation factor 3. Although the assembly pathway of the 20S and the base are well described, that of the lid is still unclear. In this study, we dissected the lid assembly using yeast lid mutant cells, rpn7-3, Delta rpn9, and rpn12-1. Using mass spectrometry, we identified a number of lid subassemblies, such as Rpn3-Rpn7 pair and a lid-like complex lacking Rpn12, in the mutants. Our analysis suggests that the assembly of the lid is a highly ordered and multi-step process; first, Rpn5, 6, 8, 9, and 11 are assembled to form a core module, then a second module, consisting of Rpn3, 7, and Semi, is attached, followed by the incorporation of Rpn12 to form the lid complex. (C) 2010 Elsevier Inc. All rights reserved.