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

Yoko Hirano; Klavs B. Hendil; Hideki Yashiroda; Lemura Shun-ichiro; Ryoichi Nagane; Yusaku Hioki; Tohru Natsume; Keiji Tanaka; Shigeo Murata

doi:10.1038/nature04106

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

Yoko Hirano, Klavs B. Hendil, Hideki Yashiroda, Lemura Shun-ichiro, Ryoichi Nagane, Yusaku Hioki, Tohru Natsume, Keiji Tanaka, Shigeo Murata

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review

214 Citationer (Scopus)

Abstract

Udgivelsesdato: 27 October 2005

Originalsprog	Engelsk
Tidsskrift	Nature
Vol/bind	437
Udgave nummer	7063
Sider (fra-til)	1381-1385
ISSN	0028-0836
DOI	https://doi.org/10.1038/nature04106
Status	Udgivet - 2005

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@article{02b0bb106c3711dcbee902004c4f4f50,

title = "A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes",

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, 1-71-71-71-7 (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 -ring formation and keeps the -rings competent for the subsequent formation of half-proteasomes. Thus, our results identify a mechanism for the correct assembly of 20S proteasomes.",

author = "Yoko Hirano and Hendil, {Klavs B.} and Hideki Yashiroda and Lemura Shun-ichiro and Ryoichi Nagane and Yusaku Hioki and Tohru Natsume and Keiji Tanaka and Shigeo Murata",

year = "2005",

doi = "10.1038/nature04106",

language = "English",

volume = "437",

pages = "1381--1385",

journal = "Nature",

issn = "0028-0836",

publisher = "nature publishing group",

number = "7063",

}

TY - JOUR

T1 - A heterodimeric complex that promotes the assembly of mammalian 20S proteasomes

AU - Hirano, Yoko

AU - Hendil, Klavs B.

AU - Yashiroda, Hideki

AU - Shun-ichiro, Lemura

AU - Nagane, Ryoichi

AU - Hioki, Yusaku

AU - Natsume, Tohru

AU - Tanaka, Keiji

AU - Murata, Shigeo

PY - 2005

Y1 - 2005

N2 - 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, 1-71-71-71-7 (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 -ring formation and keeps the -rings competent for the subsequent formation of half-proteasomes. Thus, our results identify a mechanism for the correct assembly of 20S proteasomes.

AB - 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, 1-71-71-71-7 (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 -ring formation and keeps the -rings competent for the subsequent formation of half-proteasomes. Thus, our results identify a mechanism for the correct assembly of 20S proteasomes.

U2 - 10.1038/nature04106

DO - 10.1038/nature04106

M3 - Journal article

C2 - 16251969

SN - 0028-0836

VL - 437

SP - 1381

EP - 1385

JO - Nature

JF - Nature

IS - 7063

ER -