In vitro reconstitution of eukaryotic proteasome
| Project/Area Number |
23657080
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | University of Hyogo |
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Principal Investigator |
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| Co-Investigator(Renkei-kenkyūsha) |
KATO Koichi 大学共同利用機関法人自然科学研究機構, 岡崎共通研究施設・岡崎統合バイオサイエンス, 教授 (20211849)
YAGI Hirokazu 名古屋市立大学, 大学院・薬学研究科, 助教 (70565423)
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| Project Period (FY) |
2011 – 2012
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| Project Status |
Completed (Fiscal Year 2012)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2012: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2011: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 分子認識及び相互作用 / プロテアソーム / 超分子複合体 / シャペロン / X線結晶構造解析 / 構造生物学 |
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| Research Abstract |
The eukaryotic 20S proteasome is composed of 28 subunits arranged in a cylindrical particle as four heteroheptameric rings, α(1-7)β(1-7)β(1-7)α(1-7). To elucidate the mechanisms of proteasome assembly, we performed in vitro reconstitution experiments using separately purified subunits. In the result, we showed that the α-ring is stabilized by the binding of β subunits. Furthermore, we determined the crystal structures of the Hsm3, Hsm3-Rpt1-C complex and Rpn14 E384A mutant, respectively.
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Report
(3 results)
Research Products
(20 results)
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[Journal Article] New crystal structure of proteasome-dedicated chaperone Rpnl4 at 1.6 Å resolution.2012
Author(s)
Kim, S., Nishide, A., Saeki, Y., Takagi, K., Tanaka, K., Kato, K., Mizushima, T.
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Journal Title
Acta Cryst F
Volume: 68
Issue: 5
Pages: 517-521
DOI
Related Report
Peer Reviewed
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[Journal Article] Structural basis for specific recognition of Rpt1, an ATPase subunit of the 26S proteasome, by a proteasome-dedicated chaperone Hsm32012
Author(s)
Takagi K., Kim S., Yukii H., Ueno M., Morishita R., Endo Y., Kato K., Tanaka K., Saeki Y., Mizushima T.
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Journal Title
J.Biol.Chem
Volume: 287
Issue: 15
Pages: 12172-12182
DOI
Related Report
Peer Reviewed
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