Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 15, Issue 3, Pages 228-236Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.1386
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Eukaryotic 20S proteasomes are composed of two alpha-rings and two beta-rings, which form an alpha beta beta alpha stacked structure. Here we describe a proteasome-specific chaperone complex, designated Dmp1-Dmp2, in budding yeast. Dmp1-Dmp2 directly bound to the alpha 5 subunit to facilitate alpha-ring formation. In Delta dmp1 cells, alpha-rings lacking alpha 4 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-alpha 5 complex reveals how this chaperone functions in proteasome assembly and why it dissociates from proteasome precursors before the b-rings are assembled.
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