Flagellar filament structure and cell motility of Salmonella typhimurium mutants lacking part of the outer domain of flagellin.
We have isolated spontaneous mutants of Salmonella typhimurium which can swim in the presence of antifilament antibodies. The molecular masses of flagellins isolated from these mutants were smaller than that (52 kDa) of wild-type flagellin. Two mutants which produced the smallest flagellins (42 and 41 kDa) were selected, and the domain structures of the flagellins were analyzed by trypsin digestion and then subjected to amino acid sequencing. The two flagellins have deletions at Ala-204 to Lys-292 and Thr-183 to Lys-279, respectively. These deleted parts belong to the outer domain (D3) of flagellin, which is believed to be at the surface of the filament. These mutant filaments aggregated side by side in the presence of salt, resulting in disordered motility.
Yoshioka
K
K
National Institute of Bioscience and Human-Technology, A.I.S.T., M.I.T.I., Ibaraki, Japan.
Aizawa
S
S
Yamaguchi
S
S
D000595:Amino Acid Sequence; D002465:Cell Movement / Q000235:genetics*; D005407:Flagella / Q000235:genetics / Q000648:ultrastructure*; D005408:Flagellin / Q000737:chemistry / Q000235:genetics*; D008239:Lysine / Q000031:analogs & derivatives / Q000032:analysis; D008969:Molecular Sequence Data; D009154:Mutation; D011110:Polymorphism, Genetic; D012486:Salmonella typhimurium / Q000235:genetics / Q000502:physiology* / Q000648:ultrastructure; D017421:Sequence Analysis; D017384:Sequence Deletion
C005205:epsilon-N-methyllysine; D005408:Flagellin; D008239:Lysine