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 | |
| Publication status | Published - 2010 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Physics and Astronomy(all)
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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
}
TY - JOUR
T1 - SANS investigation of assembly state of proteasome activator 28 and the 20S proteasome
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
Y1 - 2010
N2 - 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.
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.
UR - http://www.scopus.com/inward/record.url?scp=78651089981&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=78651089981&partnerID=8YFLogxK
U2 - 10.1088/1742-6596/247/1/012020
DO - 10.1088/1742-6596/247/1/012020
M3 - Article
AN - SCOPUS:78651089981
VL - 247
JO - Journal of Physics: Conference Series
JF - Journal of Physics: Conference Series
SN - 1742-6588
M1 - 012020
ER -