Department of Molecular Biosciences, Kyoto Sangyo University, Motoyama Kamigamo, Kita-ku, Kyoto, Japan.
PLoS One. 2013 May 28;8(5):e64695. doi: 10.1371/journal.pone.0064695. Print 2013.
The V1- and F1- rotary ATPases contain a rotor that rotates against a catalytic A3B3 or α3β3 stator. The rotor F(1-γ) or V1-DF is composed of both anti-parallel coiled coil and globular-loop parts. The bacterial flagellar type III export apparatus contains a V1/F1-like ATPase ring structure composed of FliI6 homo-hexamer and FliJ which adopts an anti-parallel coiled coil structure without the globular-loop part. Here we report that FliJ of Salmonella enterica serovar Typhimurium shows a rotor like function in Thermus thermophilus A3B3 based on both biochemical and structural analysis. Single molecular analysis indicates that an anti-parallel coiled-coil structure protein (FliJ structure protein) functions as a rotor in A3B3. A rotary ATPase possessing an F1-γ-like protein generated by fusion of the D and F subunits of V1 rotates, suggesting F(1-γ) could be the result of a fusion of the genes encoding two separate rotor subunits. Together with sequence comparison among the globular part proteins, the data strongly suggest that the rotor domains of the rotary ATPases and the flagellar export apparatus share a common evolutionary origin.
V1-和 F1-旋转 ATP 酶包含一个相对于催化 A3B3 或 α3β3 定子旋转的转子。转子 F(1-γ)或 V1-DF 由反平行的螺旋线圈和球状环部分组成。细菌鞭毛 III 型输出装置包含一个由 FliI6 同六聚体和 FliJ 组成的 V1/F1 样 ATP 酶环结构，它采用反平行的螺旋线圈结构，没有球状环部分。在这里，我们报道了沙门氏菌肠炎血清型的 FliJ 在基于生物化学和结构分析的嗜热栖热菌 A3B3 中显示出转子样功能。单分子分析表明，一种反平行的螺旋线圈结构蛋白（FliJ 结构蛋白）在 A3B3 中作为转子发挥作用。一个融合了 V1 的 D 和 F 亚基的产生的 F1-γ 样蛋白的旋转 ATP 酶表明，F(1-γ)可能是两个独立的转子亚基基因融合的结果。结合球状部分蛋白的序列比较，这些数据强烈表明旋转 ATP 酶和鞭毛输出装置的转子结构域具有共同的进化起源。
