Molecular architecture and assembly of the eukaryotic proteasome.
Molecular architecture and assembly of the eukaryotic proteasome.
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DOI：
10.1146/annurev-biochem-060410-150257
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发表时间：
2013
影响因子：
16.6
通讯作者：
Hochstrasser M
中科院分区：
文献类型：
--
作者：
Tomko RJ Jr;Hochstrasser M
真核泛素蛋白酶体系统负责大多数细胞质量控制和调节蛋白质降解。其底物通常由泛素聚合物修饰，最终被 26S 蛋白酶体降解。该2.6MDa蛋白质复合物被分离成具有28个亚基的桶形蛋白水解20S核心颗粒(CP)，其一端或两端被包含至少19个亚基的19S调节颗粒(RP)封端。 RP 协调底物识别、底物多聚泛素链的去除以及底物解折叠和易位到 CP 中进行降解。虽然 CP 的许多原子结构已经确定，但 RP 却难以进行高分辨率分析。然而，最近，结合冷冻电子显微镜 (cryo-EM)、生化分析和几个 RP 亚基的晶体结构测定，已经获得了大部分复合物的近原子分辨率视图。最近还对伴侣辅助蛋白酶体组装提出了重大新见解。在这里，我们回顾一下这些新颖的发现。
The eukaryotic ubiquitin-proteasome system is responsible for most cellular quality-control and regulatory protein degradation. Its substrates, which are usually modified by polymers of ubiquitin, are ultimately degraded by the 26S proteasome. This 2.6 MDa protein complex is separated into a barrel-shaped proteolytic 20S core particle (CP) of 28 subunits capped on one or both ends by a 19S regulatory particle (RP) comprising at least 19 subunits. The RP coordinates substrate recognition, removal of substrate polyubiquitin chains, and substrate unfolding and translocation into the CP for degradation. While many atomic structures of the CP have been determined, the RP has resisted high-resolution analysis. Recently, however, a combination of cryo-electron microscopy (cryo-EM), biochemical analysis, and crystal structure determination of several RP subunits has yielded a near-atomic resolution view of much of the complex. Major new insights into chaperone-assisted proteasome assembly have also recently been made. Here we review these novel findings.
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影响因子：
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DOI：
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发表时间：
2010-06-11
影响因子：
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作者：
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