Effects of mot gene expression on the structure of the flagellar motor.
Direct freezing procedures have enabled us to visualize distinctive intramembrane particle ring structures in the cytoplasmic membranes of peritrichously flagellated bacteria by means of freeze-fracture electron microscopy. These structures were identified as flagellar motor components because their distribution matched that of flagella, and because they were absent in non-flagellated mutants of Escherichia coli. Particle rings were present in both the Gram-positive Streptococcus and the Gram-negative E. coli. In E. coli, a non-functional mocha operon produced flagellated but immotile cells lacking the particle rings. Simultaneous introduction of the motA and motB genes, led to recovery of both motility and the ring structures but neither gene alone was sufficient. The concomitant loss of the rings and motility is consistent with the ring particles having a central role in the flagellar motor.
D004926:Escherichia coli / Q000648:ultrastructure; D005407:Flagella / Q000648:ultrastructure*; D005614:Freeze Fracturing; D005796:Genes; D008854:Microscopy, Electron; D013291:Streptococcus / Q000648:ultrastructure