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Subunit–subunit interactions in the human 26S proteasome
Author(s) -
Chen Chuan,
Huang Caoxin,
Chen Shouhui,
Liang Jie,
Lin Wenbo,
Ke Guifen,
Zhang Hongxin,
Wang Bing,
Huang Jian,
Han Zeguang,
Ma Lixin,
Huo Keke,
Yang Xiaoming,
Yang Pengyuan,
He Fuchu,
Tao Tao
Publication year - 2008
Publication title -
proteomics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.26
H-Index - 167
eISSN - 1615-9861
pISSN - 1615-9853
DOI - 10.1002/pmic.200700588
Subject(s) - proteasome , protein subunit , orfs , proteolysis , ubiquitin , yeast , function (biology) , biology , microbiology and biotechnology , chemistry , biochemistry , genetics , computational biology , gene , enzyme , peptide sequence , open reading frame
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 β‐rings of the 20S catalytic particle and therefore proposed a modified model of the 26S proteasome.