Formation mechanism of proteasome granules
Project/Area Number |
24657097
|
Research Category |
Grant-in-Aid for Challenging Exploratory Research
|
Allocation Type | Single-year Grants |
Research Field |
Functional biochemistry
|
Research Institution | Tokyo Metropolitan Institute of Medical Science |
Principal Investigator |
SAEKI Yasushi 公益財団法人東京都医学総合研究所, 生体分子先端研究分野, 副参事研究員 (80462779)
|
Project Period (FY) |
2012-04-01 – 2014-03-31
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥4,030,000 (Direct Cost: ¥3,100,000、Indirect Cost: ¥930,000)
Fiscal Year 2013: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2012: ¥2,600,000 (Direct Cost: ¥2,000,000、Indirect Cost: ¥600,000)
|
Keywords | 細胞内タンパク質分解 / ユビキチン / プロテアソーム / 酵母 / 可逆性顆粒 / 蛍光相関分光法 / ミトコンドリア / ATP |
Research Abstract |
The proteasome is an ATP-dependent protease complex responsible for targeted protein degradation in eukaryotic cells. To identify factors that affect the proteasome dynamics, we screened a yeast mutant library and found that the proteasome formed a large cytoplasmic granule in almost all the mitochondrial mutants. We found that lowered cellular ATP levels induce the granule formation of the proteasome even in the wild-type cells. Importantly, the granule formation of the proteasome is conserved in yeast and humans. Furthermore, the purified proteasomes formed fibrous aggregated structures by ATP depletion. Taken together, these results suggest that the proteasome itself senses cellular ATP levels and autonomously forms reversible granule structure in responding to cellular environments.
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Report
(3 results)
Research Products
(42 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] Quantitative live-cell imaging reveals spatio-temporal dynamics and cytoplasmic assembly of the 26S proteasome2014
Author(s)
Pack, CG., Yukii, H., Toh-e, A., Kudo, T., Tsuchiya, H., Kaiho, A., Sakata, E., Murata, S., Sako, Y., Baumeister, W., Tanaka, K., and Saeki, Y.
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Journal Title
Nature Commun
Volume: 5
Issue: 1
Pages: 3396-3396
DOI
Related Report
Peer Reviewed
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[Journal Article] A multi-purpose fusion tag derived from an unstructured and hyper-acidic region of the amyloid precursor protein.2013
Author(s)
Sangawa, T., Tabata, S., Suzuki, K., Saeki, Y., Tanaka, K., and Takagi, J.
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Journal Title
Protein Science
Volume: 22
Issue: 6
Pages: 840-850
DOI
Related Report
Peer Reviewed
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