A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes

Yuko Hirano, Klavs B. Hendil, Hideki Yashiroda, Shun-ichiro Iemura, Ryoichi Nagane, Yusaku Hioki, Tohru Natsume, Keiji Tanaka () and Shigeo Murata ()
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Yuko Hirano: Tokyo Metropolitan Institute of Medical Science
Klavs B. Hendil: University of Copenhagen
Hideki Yashiroda: Tokyo Metropolitan Institute of Medical Science
Shun-ichiro Iemura: Biological Information Research Center
Ryoichi Nagane: Biological Information Research Center
Yusaku Hioki: Biological Information Research Center
Tohru Natsume: Biological Information Research Center
Keiji Tanaka: Tokyo Metropolitan Institute of Medical Science
Shigeo Murata: Tokyo Metropolitan Institute of Medical Science

Nature, 2005, vol. 437, issue 7063, 1381-1385

Abstract: Abstract The 26S proteasome is a multisubunit protease responsible for regulated proteolysis in eukaryotic cells1,2. It comprises one catalytic 20S proteasome and two axially positioned 19S regulatory complexes3. The 20S proteasome is composed of 28 subunits arranged in a cylindrical particle as four heteroheptameric rings, α1–7β1–7β1–7α1–7 (refs 4, 5), but the mechanism responsible for the assembly of such a complex structure remains elusive. Here we report two chaperones, designated proteasome assembling chaperone-1 (PAC1) and PAC2, that are involved in the maturation of mammalian 20S proteasomes. PAC1 and PAC2 associate as heterodimers with proteasome precursors and are degraded after formation of the 20S proteasome is completed. Overexpression of PAC1 or PAC2 accelerates the formation of precursor proteasomes, whereas knockdown by short interfering RNA impairs it, resulting in poor maturation of 20S proteasomes. Furthermore, the PAC complex provides a scaffold for α-ring formation and keeps the α-rings competent for the subsequent formation of half-proteasomes. Thus, our results identify a mechanism for the correct assembly of 20S proteasomes.

Date: 2005
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DOI: 10.1038/nature04106

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