SANS investigation of assembly state of proteasome activator 28 and the 20S proteasome

Masaaki Sugiyama; Eiji Kurimoto; Hiroki Sahashi; Eri Sakata; Yukio Morimoto; Keiji Itoh; Kazuhiro Mori; Toshiharu Fukunaga; Yasufumi Minami; Koichi Kato

doi:10.1088/1742-6596/247/1/012020

SANS investigation of assembly state of proteasome activator 28 and the 20S proteasome

Masaaki Sugiyama, Eiji Kurimoto, Hiroki Sahashi, Eri Sakata, Yukio Morimoto, Keiji Itoh, Kazuhiro Mori, Toshiharu Fukunaga, Yasufumi Minami, Koichi Kato

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

The state of proteasome activator 28 (PA28) and the formation of the proteasomal complex in an aqueous solution are investigated with small-angle neutron scattering (SANS). The most appropriate state of PA28, which well reproduces the observed SANS profile, is the dissociation equilibrium between dimer and monomer with dissociation degree of 0.5. In addition, it is revealed that the packing of PA28 in the dimer is same as that in a crystal. It is also revealed that the proteasomal complex in which two PA28s connects to both basal planes of the 20S proteasome is spontaneously formed in the mixture solution of PA28 and the 20S proteasome.

Original language	English
Article number	012020
Journal	Journal of Physics: Conference Series
Volume	247
DOIs	https://doi.org/10.1088/1742-6596/247/1/012020
Publication status	Published - 2010

ASJC Scopus subject areas

Physics and Astronomy(all)

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10.1088/1742-6596/247/1/012020

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SANS investigation of assembly state of proteasome activator 28 and the 20S proteasome. / Sugiyama, Masaaki; Kurimoto, Eiji; Sahashi, Hiroki; Sakata, Eri; Morimoto, Yukio; Itoh, Keiji; Mori, Kazuhiro; Fukunaga, Toshiharu; Minami, Yasufumi; Kato, Koichi.

In: Journal of Physics: Conference Series, Vol. 247, 012020, 2010.

Research output: Contribution to journal › Article › peer-review

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abstract = "The state of proteasome activator 28 (PA28) and the formation of the proteasomal complex in an aqueous solution are investigated with small-angle neutron scattering (SANS). The most appropriate state of PA28, which well reproduces the observed SANS profile, is the dissociation equilibrium between dimer and monomer with dissociation degree of 0.5. In addition, it is revealed that the packing of PA28 in the dimer is same as that in a crystal. It is also revealed that the proteasomal complex in which two PA28s connects to both basal planes of the 20S proteasome is spontaneously formed in the mixture solution of PA28 and the 20S proteasome.",

author = "Masaaki Sugiyama and Eiji Kurimoto and Hiroki Sahashi and Eri Sakata and Yukio Morimoto and Keiji Itoh and Kazuhiro Mori and Toshiharu Fukunaga and Yasufumi Minami and Koichi Kato",

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AU - Sugiyama, Masaaki

AU - Kurimoto, Eiji

AU - Sahashi, Hiroki

AU - Sakata, Eri

AU - Morimoto, Yukio

AU - Itoh, Keiji

AU - Mori, Kazuhiro

AU - Fukunaga, Toshiharu

AU - Minami, Yasufumi

AU - Kato, Koichi

PY - 2010

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AB - The state of proteasome activator 28 (PA28) and the formation of the proteasomal complex in an aqueous solution are investigated with small-angle neutron scattering (SANS). The most appropriate state of PA28, which well reproduces the observed SANS profile, is the dissociation equilibrium between dimer and monomer with dissociation degree of 0.5. In addition, it is revealed that the packing of PA28 in the dimer is same as that in a crystal. It is also revealed that the proteasomal complex in which two PA28s connects to both basal planes of the 20S proteasome is spontaneously formed in the mixture solution of PA28 and the 20S proteasome.

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