he hook-basal body (HBB) complex is a multi-component structure which comprises a significant part of the bacterial flagellar motor.;I have purified and characterized HBB complexes lacking either the L ring or both the P and L rings, and concluded that the 27-kDa basal-body protein is the major component of the L ring, and that the 38-kDa basal-body protein is the major component of the P ring.;I have sequenced the genes encoding the subunit proteins of the M, P, and L rings of the basal body, and have examined both the gene and deduced amino acid sequences for clues regarding the regulation of these genes and the structure of their products.;By quantitating the amount of ;Electrophoretic mobility shifts of HBB complex component proteins from four non-flagellate mutants have enabled me to assign each protein as being the product of the gene defective in each of the respective strains.;I have developed a protocol for differential
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