| Budget Amount *help |
¥4,810,000 (Direct Cost: ¥3,700,000、Indirect Cost: ¥1,110,000)
Fiscal Year 2017: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
Fiscal Year 2016: ¥1,820,000 (Direct Cost: ¥1,400,000、Indirect Cost: ¥420,000)
Fiscal Year 2015: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
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| Outline of Final Research Achievements |
Signal-transduction regulatory systems for certain cellular responses which rely on phosphorylation of histidine or aspartic acid have known in eukaryotic cells. Identification of site-specific phosphorylation dynamics of His or Asp is technically difficult because of the labile nature of the phosphorylated amino acid residues. ATPgammaS, which used as a phosphoryl donor to trace protein kinase activities, has the advantage of permitting study of His- or Asp phosphorylation, because the resulting thiophosphorylated substrates are resistant to chemical hydrolysis or the action of phosphatases. Using the phosphate affinity electrophoresis, Phos-tag SDS-PAGE, we separated thiophosphorylated substrate generated as a intermediate of kinase reaction，and studied the dynamics of the histidine kinase reactions.
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