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Crystal structure of a chaperone complex that contributes to the assembly of yeast 20S proteasomes.

Authors
  • 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
Type
Published Article
Journal
Nature Structural & Molecular Biology
Publisher
Springer Nature
Publication Date
Mar 01, 2008
Volume
15
Issue
3
Pages
228–236
Identifiers
DOI: 10.1038/nsmb.1386
PMID: 18278057
Source
Medline
License
Unknown

Abstract

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. Dmp1-Dmp2 interacted with proteasome precursors early during proteasome assembly and dissociated from the precursors before the formation of half-proteasomes. Notably, the crystallographic structures of Dmp1 and Dmp2 closely resemble that of PAC3-a mammalian proteasome-assembling chaperone; nonetheless, neither Dmp1 nor Dmp2 showed obvious sequence similarity to PAC3. The structure of the Dmp1-Dmp2-alpha5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the beta-rings are assembled.

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