Homma M, Aizawa S, Dean G E, Macnab R M
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.
Proc Natl Acad Sci U S A. 1987 Nov;84(21):7483-7. doi: 10.1073/pnas.84.21.7483.
The M ring is a substructure of the flagellar basal body of bacteria, which lies in the cytoplasmic membrane and is therefore close to the site where the energy of the transmembrane proton potential is converted into mechanical work of rotation of the motor. The protein from which this ring is constructed has not been identified. Flagellar hook-basal body complexes from Salmonella typhimurium were used as the immunogen for the preparation of monoclonal antibodies. An antibody obtained was directed against a major basal-body component, a 65-kDa protein that from mutant studies has been assigned as the product of the flaAII.1 gene. By immunoelectron microscopy, the antibody was observed to bind the innermost feature of the basal body: the cytoplasmic-facing surface of the M ring. We conclude that the 65-kDa protein is a component--probably the main component--of this important substructure of the flagellar motor.
M环是细菌鞭毛基体的一个亚结构,它位于细胞质膜中,因此靠近跨膜质子电位的能量转化为马达旋转机械功的部位。构成这个环的蛋白质尚未被鉴定出来。鼠伤寒沙门氏菌的鞭毛钩-基体复合物被用作制备单克隆抗体的免疫原。获得的一种抗体针对一种主要的基体成分,一种65 kDa的蛋白质,通过突变研究已将其指定为flaAII.1基因的产物。通过免疫电子显微镜观察到,该抗体结合基体的最内层结构:M环面向细胞质的表面。我们得出结论,65 kDa的蛋白质是鞭毛马达这一重要亚结构的一个成分——可能是主要成分。