2013 Fiscal Year Final Research Report
Structural biology study of the ER-associated degradation machinery based on eukaryotic thermophile genomic information
| Project/Area Number |
24770102
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| Research Category |
Grant-in-Aid for Young Scientists (B)
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| Allocation Type | Multi-year Fund |
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| Research Field |
Structural biochemistry
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| Research Institution | Nagoya City University |
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Principal Investigator |
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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| Keywords | 好熱性真核生物 / 立体構造解析 / PDI / グルコシダーゼ |
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| Research Abstract |
In this study, we aimed to understand the molecular recognition and operating mechanisms of quality control machineries responsible for the glycoprotein fate determination (folding, transport, and degradation) in the endoplasmic reticulum. Our distinctive approach includes application of the genome information of eukaryotic thermophiles that can grow at high temperature (about 60 degrees Celsius). Using X-ray crystallography, we successfully determined the first crystal structures of protein disulfide isomerase (PDI) catalyzing disulfide bond formation and isomerization, and the catalytic domain of glycoprotein processing enzyme glucosidase II.
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[Journal Article] Structural basis for proteasome formation controlled by an assembly chaperone Nas22014
Author(s)
T. Satoh, Y. Saeki, T. Hiromoto, Y.-H. Wang, Y. Uekusa, H. Yagi, H. Yoshihara, M. Yagi-Utsumi, T. Mizushima, K. Tanaka, and K. Kato
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Journal Title
Structure
Volume: (in press)
DOI
Peer Reviewed
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[Journal Article] ATPase activity and ATP-dependent conformational change in the co-chaperone HSP70/HSP90-organizing protein (HOP)2014
Author(s)
S. Yamamoto, GP. Subedi, S. Hanashima, T. Satoh, M. Otaka, H. Wakui, K. Sawada, S. Yokota, Y. Yamaguchi, H. Kubota, H. Itoh
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Journal Title
J. Biol. Chem.
Volume: (in press)
Peer Reviewed
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