Subunit-subunit interactions in the human 26S proteasome
Date
2008Author
Chen, Chuan
Huang, Caoxin
Lin, Wenbo
Ke, Guifen
Zhang, Hongxin
Tao, Tao
陶涛
Chen, Shouhui(Zhongshan Hosp Xiamen)
Wang, Bing(Med Sch Xiamen)
Huang, Jian(Natl Ctr Genom)
Han, Zeguang(Natl Ctr Genom)
Ma, Lixin(Hubei Univ)
Huo, Keke(Fudan Univ)
Yang, Pengyuan(Fudan Univ)
He, Fuchu( Beijing Proteom Ctr)
Collections
- 生命科学-已发表论文 [5901]
Abstract
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.