Structural insight into proteasome orchestration controlled by assembly chaperone Nas2
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چکیده
Tadashi Satoh, Yasushi Saeki, Takeshi Hiromoto, Ying-Hui Wang, Yoshinori Uekusa, Hirokazu Yagi, Hidehito Yoshihara, Maho Yagi-Utsumi, Tsunehiro Mizushima, Keiji Tanaka, and Koichi Kato Graduate School of Pharmaceutical Sciences, Nagoya City University, Nagoya 467-8603, Japan JST, PRESTO, Nagoya 467-8603, Japan Tokyo Metropolitan Institute of Medical Science, Tokyo 156-8506, Japan Okazaki Institute for Integrative Bioscience, Okazaki 444-8787, Japan Graduate School of Life Science, University of Hyogo, Hyogo 678-1297, Japan
منابع مشابه
1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain
The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to the C-terminal tail of Rpt5; however, it does not require the C-ter...
متن کاملX 1 . 15 Å resolution structure of the proteasome - assembly chaperone Nas 2 PDZ domain
PDB reference: proteasome-assembly chaperone Nas2 PDZ domain, 4o06 The 26S proteasome is a 2.5 MDa protease dedicated to the degradation of ubiquitinated proteins in eukaryotes. The assembly of this complex containing 66 polypeptides is assisted by at least nine proteasome-specific chaperones. One of these, Nas2, binds to the proteasomal AAA-ATPase subunit Rpt5. The PDZ domain of Nas2 binds to ...
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The proteasome is assembled via the nine-subunit lid, nine-subunit base, and 28-subunit core particle (CP). Previous work has shown that the chaperones Rpn14, Nas6, Hsm3, and Nas2 each bind a specific ATPase subunit of the base and antagonize base-CP interaction. Here, we show that the Nas6 chaperone also obstructs base-lid association. Nas6 alternates between these two inhibitory modes accordi...
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Assembly of the eukaryotic 20S proteasome is an ordered process involving several proteins operating as proteasome assembly factors including PAC1-PAC2 but archaeal 20S proteasome subunits can spontaneously assemble into an active cylindrical architecture. Recent bioinformatic analysis identified archaeal PAC1-PAC2 homologs PbaA and PbaB. However, it remains unclear whether such assembly factor...
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The ubiquitin-proteasome proteolytic pathway is pivotal in most biological processes. Despite a great level of information available for the eukaryotic 26S proteasome-the protease responsible for the degradation of ubiquitylated proteins-several structural and functional questions remain unanswered. To gain more insight into the assembly and function of the metazoan 26S proteasome, a two-hybrid...
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تاریخ انتشار 2014