Localization of proteins controlling motility and chemotaxis in Escherichia coli

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Abstract
Flagellar proteins controlling motility and chemotaxis in E. coli were selective labeled in vivo with [35S]methionine. This distribution of these proteins in subcellular fractions was examined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. The motA, motB, cheM and cheD gene products were confined exclusively to the inner cytoplasmic membrane fraction, but the cheY, cheW and cheA (66,000 daltons) polypeptides appeared only in the soluble cytoplasmic fraction. The cheB, cheX, cheZ and cheA (76,000 daltons) proteins were distributed in the cytoplasm and the inner membrane fractions. The hag gene product (flagellin) was the only flagellar protein examined that copurified with the outer lipopolysaccharide membrane. Differences in the intracellular locations of the che and mot gene products presumably reflect the functional attributes of these components.