Article
Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes.
Nature structural & molecular biology - 1 Mar 2008
Yashiroda Hideki, Mizushima Tsunehiro, Okamoto Kenta, Kameyama Tomie, Hayashi Hidemi, Kishimoto Toshihiko, Niwa Shin-ichiro, Kasahara Masanori, Kurimoto Eiji, Sakata Eri, Takagi Kenji, Suzuki Atsuo, Hirano Yuko, Murata Shigeo, Kato Koichi, Yamane Takashi, Tanaka Keiji
Abstract excerpt
Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alphabetabetaalpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha5 subunit to facilitate alpha-ring formation. In Deltadmp1 cells, alpha-rings lacking alpha4 and decreased formation of 20S proteasomes were observed....
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