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  • Title: Subunit-subunit interactions in the human 26S proteasome.
    Author: Chen C, Huang C, Chen S, Liang J, Lin W, Ke G, Zhang H, Wang B, Huang J, Han Z, Ma L, Huo K, Yang X, Yang P, He F, Tao T.
    Journal: Proteomics; 2008 Feb; 8(3):508-20. PubMed ID: 18186020.
    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 beta-rings of the 20S catalytic particle and therefore proposed a modified model of the 26S proteasome.
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