Subunit-subunit interactions in the human 26S proteasome.
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 beta-rings of the 20S catalytic particle and therefore proposed a modified model of the 26S proteasome.
Chen
Chuan
C
Key Laboratory for Cell Biology and Tumor Cell Engineering, the Ministry of Education, School of Life Sciences, Xiamen University, Xiamen, China.
Huang
Caoxin
C
Chen
Shouhui
S
Liang
Jie
J
Lin
Wenbo
W
Ke
Guifen
G
Zhang
Hongxin
H
Wang
Bing
B
Huang
Jian
J
Han
Zeguang
Z
Ma
Lixin
L
Huo
Keke
K
Yang
Xiaoming
X
Yang
Pengyuan
P
He
Fuchu
F
Tao
Tao
T
D006801:Humans; D008954:Models, Biological; D016366:Open Reading Frames / Q000235:genetics; D046988:Proteasome Endopeptidase Complex / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology*; D021122:Protein Subunits / Q000235:genetics / Q000378:metabolism*
D021122:Protein Subunits; D046988:Proteasome Endopeptidase Complex; C061553:ATP dependent 26S protease