Clarification of molecular mechanism of bacterial divisome formation

2014 Fiscal Year Final Research Report

• Project/Area Number: 24770088
• Research Category: Grant-in-Aid for Young Scientists (B)
• Allocation Type: Multi-year Fund
• Research Field: Structural biochemistry
• Research Institution: University of Toyama
• Principal Investigator: MATSUI Takashi 富山大学, 和漢医薬学総合研究所, 助教 (30463582)
• Project Period (FY): 2012-04-01 – 2015-03-31
• Keywords: FtsZ / FtsA / 細菌の細胞分裂 / Divisome / 構造解析

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.

Free Research Field

構造生物学