Clarification of molecular mechanism of bacterial divisome formation
| Project/Area Number |
24770088
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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 | University of Toyama |
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Principal Investigator |
MATSUI Takashi 富山大学, 和漢医薬学総合研究所, 助教 (30463582)
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| Project Period (FY) |
2012-04-01 – 2015-03-31
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| Project Status |
Completed (Fiscal Year 2014)
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| Budget Amount *help |
¥4,550,000 (Direct Cost: ¥3,500,000、Indirect Cost: ¥1,050,000)
Fiscal Year 2014: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2013: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2012: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
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| Keywords | FtsZ / FtsA / 細菌の細胞分裂 / Divisome / 構造解析 / X線結晶構造解析 / 真正細菌 / 細胞分裂 / 真性細菌 / タンパク質複合体 |
|---|
| Outline of Final Research Achievements |
To clarify the mechanism of forming the bacterial divisome, firstly, FtsZ, which polymerizes as the protofilament, was crystallized and its novel conformation was determined. Moreover, it was also found that previous and novel FtsZ protomers were converted each other, and one of the potent inhibitor bound to a cleft formed on the novel protomer.
Subsequently, to determine the complex structure of FtsZ with FtsA, the conditions of FtsA under complex state were measured. Crystal structure of FtsA apo form suggested that FtsA seemed to have ATPase activity. ATPase activity of FtsA with or without FtsZ was not detected. However, polymerized FtsZ or monomeric FtsZ’s mutant bound to FtsA with 1:2 ratio of FtsA: FtsZ. It was seemed that ATPase activity might be not correlated with interaction of FtsZ.
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Report
(4 results)
Research Products
(10 results)
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[Journal Article] A peptide ligase and the ribosome cooperate to synthesize the peptide pheganomycin.2015
Author(s)
Noike, M., Matsui, T., Ooya, K., Sasaki, I., Ohtaki, S., Hamano, Y., Maruyama, C., Ishikawa, J., Satoh, Y., Ito, H., Morita, H. and Dairi T.
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Journal Title
Nature Chemical Biology
Volume: 11
Issue: 1
Pages: 71-76
DOI
NAID
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Structural basis for the formation of acylalkylpyrones from two β-ketoacyl units by the fungal type III polyketide synthase CsyB2015
Author(s)
Mori, T., Yang, D., Matsui, T, Hashimoto, M., Morita, H., Fujii, I., Abe, I.
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Journal Title
J. Biol. Chem.
Volume: 290
Issue: 8
Pages: 5214-5225
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Expression, purification, and crystallization of a fungal type III polyketide synthase that produces the csypyrones2014
Author(s)
Yang, D., Mori, T., Matsui, T., Hashimoto, M., Morita, H., Fujii, I., Abe, I.
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Journal Title
Acta Crystallogr., Sect. F: Struct. Biol. Cryst. Commun.
Volume: 70
Issue: 6
Pages: 730-733
DOI
Related Report
Peer Reviewed / Acknowledgement Compliant
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