Establishment of a quantitative method for the dynamical analysis of bacterial two-component systems toward studies on an innovative drug development
| Project/Area Number |
25560417
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| Research Category |
Grant-in-Aid for Challenging Exploratory Research
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| Allocation Type | Multi-year Fund |
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| Research Field |
Chemical biology
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| Research Institution | Hiroshima University |
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Principal Investigator |
Kinoshita Eiji 広島大学, 医歯薬保健学研究院(薬), 准教授 (80304418)
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| Project Period (FY) |
2013-04-01 – 2016-03-31
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| Project Status |
Completed (Fiscal Year 2015)
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| Budget Amount *help |
¥3,900,000 (Direct Cost: ¥3,000,000、Indirect Cost: ¥900,000)
Fiscal Year 2015: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2014: ¥1,300,000 (Direct Cost: ¥1,000,000、Indirect Cost: ¥300,000)
Fiscal Year 2013: ¥1,040,000 (Direct Cost: ¥800,000、Indirect Cost: ¥240,000)
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| Keywords | フォスタグ / ２成分伝達系 / ヒスチジンキナーゼ / レスポンスレギュレーター / 生体分子計測 / 2成分伝達系 / ヒスツジンキナーゼ |
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| Outline of Final Research Achievements |
One mode of bacterial intracellular signal transduction involves two-component regulatory systems mediated by phosphorylation of His and Asp residues. The chemical instability of phosphate groups on these residues hampers research on protein phosphorylation in such regulatory systems. In this study, Phos-tag SDS-PAGE originally developed as a novel method to research on protein phosphorylation has been applied to the dynamical analysis of two-component systems. As a result, this method permitted to identify aspects relevant to signaling molecules, including kinetic properties of enzymes and substrates in intramolecular and intermolecular phosphotransfer and autophosphorylation reactions. Furthermore, Phos-tag SDS-PAGE has been demonstrated as a useful quantitative method for the development of inhibitors of histidine kinases.
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Report
(4 results)
Research Products
(72 results)
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[Journal Article] Expression and phosphorylation state analysis of intracellular protein kinases using Multi- PK antibody and Phos- tag SDS- PAGE.2015
Author(s)
Sugiyama, Y., Katayama, S., Kameshita, I., Morisawa, K., Higuchi, T., Todaka, H., Eiji Kinoshita, Kinoshita- Kikuta, E., Koike, T., Taniguchi, T., Sakamoto, S.
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Journal Title
MethodsX
Volume: 2
Pages: 469-474
DOI
Related Report
Peer Reviewed / Open Access / Int'l Joint Research
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[Journal Article] Simple enrichment of thiol- containing biomolecules by using zinc(II)-cyclen-functionalized magnetic beads2014
Author(s)
Fujioka, H., Tsunehiro, M., Kawaguchi, M., Kuramoto, Y., Kurosaki, H., Hieda, Y., Kinoshita-Kikuta, E., Eiji Kinoshita, and Koike, T.
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Journal Title
J. Sep. Sci.
Volume: 37
Issue: 13
Pages: 1601-1609
DOI
Related Report
Peer Reviewed / Open Access / Acknowledgement Compliant
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[Journal Article] Excystment-dependent alteration of protein expression in terrestrial ciliate Colpoda cucullus.2013
Author(s)
Sogame, Y., Kojima, K., Takeshita, T., Eiji Kinoshita, Funadani, R., and Matsuoka, T.
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Journal Title
Microbes Environ.
Volume: 28
Pages: 388-390
NAID
Related Report
Peer Reviewed
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[Journal Article] Increase in Lipophilicity of Enalaprilat by Complexation with Copper(II) or Zinc(II) Ions.2013
Author(s)
Fujioka, H., Hieda, Y., Kuramoto, Y, Konishi, K., Kinoshita-Kikuta, E., Eiji Kinoshita, and Koike T.
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Journal Title
Yakugaku Zasshi
Volume: 33
Pages: 1135-1141
NAID
Related Report
Peer Reviewed
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