| 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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| 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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