| 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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| 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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