Identification and structural-functional analysis of shuttle-type proteasome activator exhibiting molecular chaperone activity
| 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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Report
(3 results)
Research Products
(38 results)
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[Journal Article] Structural Basis for Proteasome Formation Controlled by an Assembly Chaperone Nas22014
Author(s)
Satoh T, Saeki Y, Hiromoto T, Wang YH, Uekusa Y, Yagi H, Yoshihara H, Yagi-Utsumi M, Mizushima T, Tanaka K, Kato K
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Journal Title
Structure
Volume: (掲載確定)
Issue: 5
Pages: 731-743
DOI
Related Report
Peer Reviewed
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[Journal Article] Spatial arrangement and functional role of α subunits of proteasome activator PA28 in hetero-oligomeric form.2013
Author(s)
Sugiyama, M., Sahashi, H., Kurimoto, E., Takata, S., Yagi, H., Kanai, K., Sakata, E., Minami, Y., Tanaka, K., and Kato K.
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Journal Title
Biochem Biophys Res Commun.
Volume: 432
Issue: 1
Pages: 141-145
DOI
Related Report
Peer Reviewed
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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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[Presentation] An archaeal homolog of proteasome assembly chaperone forms a homotetramer and functions as proteasome activator2013
Author(s)
K. Kumoi, T. Satoh, K. Murata, T.Hiromoto, T. Mizushima, Y. Kamiya, M.Noda, S. Uchiyama, M. Sugiyama, H. Yagi,and K. Kato
Organizer
6^<th> Japan-Korea Seminars on Biomolecular Science : Experiments and Simulation
Place of Presentation
岡崎コンファレンスセンター(愛知)
Year and Date
2013-11-27
Related Report
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[Presentation] An archaeal homolog of proteasome assembly chaperone forms a homotetramer and functions as proteasome activator
Author(s)
Kentaro Kumoi, Tadashi Satoh, Kazuyoshi Murata, Takeshi Hiromoto, Tsunehiro Mizushima, Yukiko Kamiya, Masanori Noda, Susumu Uchiyama, Masaaki Sugiyama, Hirokazu Yagi, Koichi Kato
Organizer
6th Japan-Korea Seminars on Biomolecular Science: Experiments and Simulation
Place of Presentation
岡崎コンファレンスセンター（愛知県）
Related Report
Invited
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