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.
Subunit-subunit interactions in the human 26S proteasome. Publishing Authors By Initials
Subunit-subunit interactions in the human 26S proteasome. Journal Published:
PUBLICATION TYPE: Journal Article
Journal: Proteomics
VOLUME: 8
Page Numbers: 508-20
Journal Abbreviation: Proteomics
ISSN: 1615-9853
DAY: 2
MONTH: Feb
YEAR: 2008
Subunit-subunit interactions in the human 26S proteasome. Information
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LANGUAGE: eng
NlmUniqueID: 101092707
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Grant and Affiliation Information for Subunit-subunit interactions in the human 26S proteasome.
AFFILIATION: Key Laboratory for Cell Biology and Tumor Cell Engineering, the Ministry of Education, School of Life Sciences, Xiamen University, Xiamen, China.
Country: Germany
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MEDLINETA: Proteomics
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