The basal body of Wolinella succinogenes consists of a central rod, a set of two rings (L and P rings), a basal disk front 70 to 200 nm in diameter, and a terminal knob. In negatively stained preparations of flagellar hook-basal body complexes, some disks remain fixed perpendicularly to the grid and show that such a disk is located on the distal side of the P ring. The basal disks have been isolated with and without the P ring; in both cases there is a hole in the center of the disk. The diameter of the disk is smaller in the presence of the P ring. The L-P ring complex is therefore assumed to be a bushing for the rod. Thin sections of whole bacteria and spheroplasts reveal that the disk is attached to the inner surface of the outer membrane. At the insertions of the flagellar hook-basal body-basal disk complexes, depressions are visible in negatively stained preparations of whole bacteria and spheroplasts. A new ringlike structure is connected to an elongation of the basal body into the cytoplasm in both preparations. Its diameter (60 nm) is larger than that of the M ring. A heavily stained compartment can be seen in between the new ringlike structure and the basal disk, which may be formed by the energy transducing units.For a long time the entity called the intact flagellum (6-8) was thought to be the essential rotary device of the flagellar motor. In Escherichia coli and Salmonella typhimurium, this assembly consists of the flagellar filament, the hook, and the basal body. The basal body appears as a set of four rings coaxial with the rod. Two rings are very likely to be correlated to membranes: the L ring to the outer membrane and the M ring to the inner membrane. The P ring is in the periplasmic space and is assumed to interact with the peptidoglycan layer. The S ring is clearly visible in negatively stained electron micrographs in both bacteria, but from genetic, biochemical, and physiological studies no indications for its existence emerged until now (10, 11). In an extensive search for flagellar and motility mutants with the paralyzed or switch-defective phenotype, none mapped to the gene of the M ring (fliF) (10); all mapped to five genes encoding proteins that are not present on isolated basal bodies. Three of them (fiG, fliM, fliN) encode flagellar components that participate in both energy transduction and switching (15), whereas the other two (motA, motB) encode proteins that appear to function in energy transduction only (5,18,21,22). It is therefore unlikely that the M ring is the active rotor of the bacterial flagellar apparatus. Furthermore, it was proposed about 13 years ago by Coulton and Murray (3, 4) that essential structures of the flagellar apparatus were lost during the procedures for isolation of intact flagella. They found circlets of about 15 particles around the rod in the cytoplasmic membrane and outer membraneassociated large disks, called concentric membrane rings, in Aquaspirillum serpens.From Wolinella succinogenes, an anaerobic, gram-negative bacterium with one polar flagellum,...