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

Author

Listed:
  • 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
    PRESTO, Japan Science and Technology Agency)

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.

Suggested Citation

  • Yuko Hirano & Klavs B. Hendil & Hideki Yashiroda & Shun-ichiro Iemura & Ryoichi Nagane & Yusaku Hioki & Tohru Natsume & Keiji Tanaka & Shigeo Murata, 2005. "A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes," Nature, Nature, vol. 437(7063), pages 1381-1385, October.
    • Handle: RePEc:nat:nature:v:437:y:2005:i:7063:d:10.1038_nature04106
    DOI: 10.1038/nature04106
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    Cited by:

    1. Kwadwo A. Opoku-Nsiah & Andres H. Pena & Sarah K. Williams & Nikita Chopra & Andrej Sali & Gabriel C. Lander & Jason E. Gestwicki, 2022. "The YΦ motif defines the structure-activity relationships of human 20S proteasome activators," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Nobuo Kanazawa & Hiroaki Hemmi & Noriko Kinjo & Hidenori Ohnishi & Jun Hamazaki & Hiroyuki Mishima & Akira Kinoshita & Tsunehiro Mizushima & Satoru Hamada & Kazuya Hamada & Norio Kawamoto & Saori Kado, 2021. "Heterozygous missense variant of the proteasome subunit β-type 9 causes neonatal-onset autoinflammation and immunodeficiency," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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