Purification and characterization of a polyhook protein from Caulobacter crescentus.
A polyhook-producing strain of Caulobacter crescentus was isolated, and the polyhook protein was purified. The antigenicity and morphology of the polyhook structure are similar to the wild-type hook except that the mutant strain produces a hook structure at least 10-fold the length of wild-type hooks (1.0 versus 0.1 micrometers). The molecular weight of the polyhook protein, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, is 72,000, and the protein has a pI of approximately 6.1. Antibodies prepared against the polyhook protein were used to show that this protein is antigenically distinct from the Caulobacter flagellins. Amino acid analysis of the polyhook protein revealed compositional similarities to other gram-negative, bacterial hook proteins.
D000596:Amino Acids / Q000032:analysis; D001419:Bacteria / Q000648:ultrastructure*; D001426:Bacterial Proteins / Q000032:analysis* / Q000276:immunology / Q000302:isolation & purification; D000939:Epitopes; D005407:Flagella / Q000648:ultrastructure; D005408:Flagellin / Q000276:immunology; D008970:Molecular Weight
D000596:Amino Acids; D001426:Bacterial Proteins; D000939:Epitopes; D005408:Flagellin