| Project/Area Number |
24657113
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Single-year Grants |
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| Research Field |
Biophysics
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| Research Institution | Okazaki Research Facilities, National Institutes of Natural Sciences |
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Principal Investigator |
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センター, 教授 (20211849)
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| Co-Investigator(Renkei-kenkyūsha) |
YAMAGUCHI Takumi 分子科学研究所, 生命・錯体分子科学研究領域, 助教 (60522430)
YAGI Maho 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センター, 特任助教 (40608999)
SATOH Tadashi 名古屋市立大学, 薬学研究科(研究院), 准教授 (80532100)
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| Project Period (FY) |
2012-04-01 – 2014-03-31
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| Project Status |
Completed (Fiscal Year 2013)
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| Budget Amount *help |
¥4,160,000 (Direct Cost: ¥3,200,000、Indirect Cost: ¥960,000)
Fiscal Year 2013: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
Fiscal Year 2012: ¥2,080,000 (Direct Cost: ¥1,600,000、Indirect Cost: ¥480,000)
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| Keywords | プロテアソーム / 4次構造 / 活性化因子 / シャペロン / 古細菌 / 四次構造 |
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| Research Abstract |
Assembly of the eukaryotic 20S proteasome is not spontaneous self-organization but an ordered process involving several assembly chaperones, whereas that of the archaeal 20S proteasome involves spontaneous self-assembly. Recent genomic analysis identified archaeal homologs of the assembly chaperones, PbaA and PbaB. However, it remains unclear how such assembly chaperone-like proteins play an indispensable role in assembly of the proteasome subunit in archaea. This study revealed that PbaB actually functions as a proteasome activator. Furthermore, our integrative biochemical and biophysical approach including X-ray crystallography, electron microscopy, NMR spectroscopy, and small-angle neutron scattering provided mechanistic clues to the molecular action of the active complex formed between the PbaB homotetramer and 20S proteasome.
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