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Studies on the membranes of Bacilli. II. Characterization of a novel protein of a Bacillus species.

Abstract During an earlier study on the localization of the enzymes of phospholipid synthesis in the ghosts of an unidentified Bacillus species (designated Bacillus PP) the presence of fibers in ghost preparations was noted. More extensive electron microscopic study has revealed the presence of large quantities of these fibers at the periphery of intact cells. The majority of the fibers were found to remain associated with the ghosts isolated from Bacillus PP. Treatment of the ghosts at pH 11 resulted in release of the fibers, which were isolated and analyzed by chemical and physical methods. Disc gel electrophoresis in two systems and gel filtration indicate that the fibers are composed of a single polypeptide of molecular weight 31,000 to 33,000. The purity of the fibers was confirmed by amino acid analysis and by fingerprint analysis after tryptic digestion. Electron microscopic examination, physical and chemical analysis, and immunological studies showed that these fibers are unrelated to the flagella of Bacillus PP. Detailed electron microscopic studies revealed that the fibers were composed of bundles of fibrils having a diameter of 30 to 40 A and a regular wavelike structure. Under certain conditions these fibrils dissociated into single filaments 12 to 15 A in diameter. The function of these fibers and the nature of their association with the cytoplasmic membrane is unknown.