TY - JOUR
T1 - Structural basis for proteasome formation controlled by an assembly chaperone Nas2
AU - Satoh, Tadashi
AU - Saeki, Yasushi
AU - Hiromoto, Takeshi
AU - Wang, Ying Hui
AU - Uekusa, Yoshinori
AU - Yagi, Hirokazu
AU - Yoshihara, Hidehito
AU - Yagi-Utsumi, Maho
AU - Mizushima, Tsunehiro
AU - Tanaka, Keiji
AU - Kato, Koichi
N1 - Funding Information:
We thank Kiyomi Senda, Kumiko Hattori, Yukiko Isono, and Hiroko Mizuki for their help in the preparation of the recombinant proteins. Diffraction data sets were collected at NSRRC using beamline 13B1 (Taiwan), Photon Factory using NE-3A (Japan) and Osaka University using BL44XU at SPring-8 equipped with MX225-HE (Rayonix), which is financially supported by Academia Sinica and NSRRC. We thank beamline staff for providing data collection facilities and support. The strain Pyrococcus furiosus (JCM 8422) was provided by Japan Collection of Microorganisms, RIKEN BRC, which participates in the National BioResource Project of the MEXT, Japan. This work was supported in part by JSPS KAKENHI (grants 25121730 to T.S., 22687009 and 24112008 to Y.S., 21000012 to K.T., and 25102008 and 24657113 to K.K.), the Okazaki ORION project, and the Nanotechnology Platform Project, and the Targeted Proteins Research Program from the Ministry of Education, Culture, Sports, Science and Technology, Japan (to K.K., K.T., and T.M.).
PY - 2014/5/6
Y1 - 2014/5/6
N2 - Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.
AB - Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.
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U2 - 10.1016/j.str.2014.02.014
DO - 10.1016/j.str.2014.02.014
M3 - Article
C2 - 24685148
AN - SCOPUS:84899918113
VL - 22
SP - 731
EP - 743
JO - Structure with Folding & design
JF - Structure with Folding & design
SN - 0969-2126
IS - 5
ER -