Waveform analysis and structure of flagella and basal complexes from Bdellovibrio bacteriovorus 109J.
The structure of sheathed flagella from Bdellovibrio bacteriovorus was investigated. The first three periods of these flagella were characterized by progressively smaller wavelengths and amplitudes in periods more distal to the cell. The damped appearance was due to a single nonrandom transition between two helical structures within each filament. The intersection of the two helices, one of which was a threefold-reduced miniature of the other, occurred at a fixed distance along the filament and resulted in a shift in the flagellar axis. Flagella increased in length as the cells aged and assumed a constant miniature waveform at their distal ends. The core filament was the principal determinant of flagellar morphology. It was composed of 28,000- and 29,500-dalton polypeptides. The 28,000-dalton subunits were located in the cell-proximal segment of the filament, and the 29,500-dalton subunits were located in the more distal region. The heteromorphous appearance of bdellovibrio flagella arose from the sequential assembly of these subunits. The basal complex associated with core filaments was examined because of its potential involvement in sheath formation. Bdellovibrio basal organelles were generally similar to those of other gram-negative species, but appeared to lack a disk analogous to the outer membrane-associated L ring which is a normal component of gram-negative basal complexes.
D001425:Bacterial Outer Membrane Proteins / Q000032:analysis; D001501:Bdellovibrio / Q000648:ultrastructure*; D002458:Cell Fractionation; D004591:Electrophoresis, Polyacrylamide Gel; D005407:Flagella / Q000648:ultrastructure*; D008854:Microscopy, Electron
D001425:Bacterial Outer Membrane Proteins