Subunit-subunit interactions in the human 26S proteasome
Subunit-subunit interactions in the human 26S proteasome
复制标题
人类 26S 蛋白酶体中的亚基-亚基相互作用
DOI：
10.1002/pmic.200700588
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发表时间：
2008-02-01
期刊：
影响因子：
3.4
通讯作者：
Tao, Tao
中科院分区：
文献类型：
--
作者：
Chen, Chuan;Huang, Caoxin;Tao, Tao
泛素依赖的蛋白分解是由蛋白酶体介导的。为了了解人类26S蛋白酶体的结构和功能，我们克隆了32个人蛋白酶体亚基的完整ORF，并对它们之间的相互作用进行了酵母双杂交分析。我们观察到在人类26S蛋白酶体中有114个相互作用对。大约10%(11/114)的相互作用对被GST-Pull-down分析所证实。在这些观察到的相互作用亚基中，58%(66/114)是新发现的，其余42%(48/114)是以前在人类或其他物种中报道的。我们观察到19S调节颗粒与20S催化颗粒的P-环之间的新的相互作用，从而提出了一个改进的26S蛋白酶体模型。
Ubiquitin-dependent proteolysis is mediated by the proteasome. To understand the structure and function of the human 26S proteasome, we cloned complete ORFs of 32 human proteasome subunits and conducted a yeast two-hybrid analysis of their interactions with each other. We observed that there are 114 interacting-pairs in the human 26S proteasome. About 10% (11/114) of these interacting-pairs was confirmed by the GST-pull down analysis. Among these observed interacting subunits, 58% (66/114) are novel and the rest 42% (48/114) has been reported previously in human or in other species. We observed new interactions between the 19S regulatory particle and the P-rings of the 20S catalytic particle and therefore proposed a modified model of the 26S proteasome.