Study on the N-terminal modification and secretory pathway of novel haloalkylphosphorus hydrolase.
| Project/Area Number |
24780096
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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 |
Applied biochemistry
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| Research Institution | Nagaoka University of Technology |
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Principal Investigator |
ABE Katsumasa 長岡技術科学大学, 工学(系)研究科(研究院), 助教 (40509551)
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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: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥2,340,000 (Direct Cost: ¥1,800,000、Indirect Cost: ¥540,000)
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| Keywords | 有機リン化合物 / 加水分解酵素 / シグナルペプチド / ピログルタミン酸 / 難分解性環境汚染物質 / ペリプラズム |
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| Outline of Final Research Achievements |
Haloalkylphosphorus hydrolase (HAD) from tris(1,3-dichloro-2-propyl) phosphate (TDCPP)-degrading bacteria, Sphingomonas sp. strain TDK1, exhibits unique properties and, therefore, is different from other bacterial organophosphorus hydrolase. In this study, I investigated the localization and the mechanism of N-terminal modification of HAD.
The genes involved in protein secretion, tatABC, secDF and secYEG, were identified in the draft genome of TDK1. Furthermore, the glutaminyl cyclase gene was also found, indicating that the N-terminal glutaminyl residue of HAD is enzymatically modified. Localization analysis of HAD in E. coli suggested that the HAD exports via Sec pathway but not Tat pathway. Deletion analysis of signal peptide of HAD showed that this sequence is crucial for the activity of HAD. Finally, the amino acid residues in the signal peptide essential for the activity HAD were identified.
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Report
(4 results)
Research Products
(22 results)
