Ito Masahiro, Terahara Naoya, Fujinami Shun, Krulwich Terry Ann
Graduate School of Life Sciences, Toyo University, Oura-gun, Gunma 374-0193, Japan.
J Mol Biol. 2005 Sep 16;352(2):396-408. doi: 10.1016/j.jmb.2005.07.030.
Bacillus subtilis has a single set of flagellar rotor proteins that interact with two distinct stator-force generators, the H+-coupled MotAB complex and the Na+-coupled MotPS complex, that energize rotation. Here, motility on soft agar plates and in liquid was assayed in wild-type B.subtilis and strains expressing only one stator, either MotAB, MotPS or hybrid MotAS or MotPB. The strains expressing MotAB or MotAS had an average of 11 flagella/cell while those expressing MotPS or MotPB had an average of seven flagella/cell, and a Mot-less double mutant had three to four flagella/cell. MotAB had a more dominant role in motility than MotPS under most conditions, but MotPS supported comparable motility to MotAB on malate-containing soft agar plating media at elevated pH and Na+. MotAB supported much faster swimming speeds in liquid than MotPS, MotAS or MotPB under all conditions, but a contribution of MotPS to wild-type swimming was discernible from differences in swimming speeds of wild-type and MotAB at elevated viscosity, pH and Na+. Swimming supported by MotPS and MotAS was stimulated by Na+ and elevated pH whereas the converse was true of MotAB and MotPB. This suggests that MotAS is Na+-coupled and MotPB is H+-coupled and that MotB and MotS are major determinants of ion-coupling. However, the swimming speed supported by MotPB, as well as MotPS and MotAS, was inhibited severely at Na+ concentrations above 300 mM whereas MotAB-dependent swimming was not. The presence of either the MotP or MotS component in the stator also conferred sensitivity to inhibition by an amiloride analogue. These observations suggest that MotP contributes to Na+-coupling and inhibition by Na+ channel inhibitors. Similarly, a role for MotA in H+-dependent stator properties is indicated by the larger effects of pH on the Na+-response of MotAS versus MotPS. Finally, optimal function at elevated viscosity was found only in MotPS and MotPB and is therefore conferred by MotP.
枯草芽孢杆菌有一套单一的鞭毛转子蛋白,可与两种不同的定子力发生器相互作用,即H⁺偶联的MotAB复合物和Na⁺偶联的MotPS复合物,它们为旋转提供能量。在此,对野生型枯草芽孢杆菌以及仅表达一种定子(MotAB、MotPS或杂交的MotAS或MotPB)的菌株在软琼脂平板和液体中的运动能力进行了测定。表达MotAB或MotAS的菌株平均每个细胞有11根鞭毛,而表达MotPS或MotPB的菌株平均每个细胞有7根鞭毛,无Mot的双突变体每个细胞有3至4根鞭毛。在大多数情况下,MotAB在运动能力方面比MotPS起更主导的作用,但在pH值和Na⁺升高的含苹果酸的软琼脂平板培养基上,MotPS支持与MotAB相当的运动能力。在所有条件下,MotAB在液体中支持的游泳速度比MotPS、MotAS或MotPB快得多,但从野生型和MotAB在粘度、pH值和Na⁺升高时游泳速度的差异可以看出MotPS对野生型游泳的贡献。MotPS和MotAS支持的游泳受到Na⁺和pH值升高的刺激,而MotAB和MotPB则相反。这表明MotAS是Na⁺偶联的,MotPB是H⁺偶联的,并且MotB和MotS是离子偶联的主要决定因素。然而,MotPB以及MotPS和MotAS支持的游泳速度在Na⁺浓度高于300 mM时受到严重抑制,而MotAB依赖的游泳则不受影响。定子中MotP或MotS成分的存在也赋予了对氨氯地平类似物抑制的敏感性。这些观察结果表明MotP有助于Na⁺偶联和Na⁺通道抑制剂的抑制作用。同样,pH值对MotAS与MotPS的Na⁺反应的较大影响表明MotA在H⁺依赖的定子特性中起作用。最后,仅在MotPS和MotPB中发现了在粘度升高时的最佳功能,因此是由MotP赋予的。