| Literature DB >> 3301807 |
M Homma, K Ohnishi, T Iino, R M Macnab.
Abstract
The flagellar genes flaFV, flaFVII, and flaFVIII of Salmonella typhimurium were cloned, and their presence on a given plasmid was verified by complementation of Escherichia coli mutants defective in the homologous genes. The gene products were identified by radiolabeling in a minicell system as being proteins of the following molecular masses: FlaFV, 42 kilodaltons (kDa); FlaFVI, 32 kDa; FlaFVII, 30 kDA; and FlaFVIII, 27 kDa. These data, together with isoelectric focusing data, confirm gene product assignments of flagellar components made indirectly from mutant studies. Flagellar components are transported by either a signal peptide-dependent or a flagellar-specific pathway. Consistent with its location in the outer membrane ring of the basal body, protein FlaFVIII seems to use the signal peptide-dependent pathway, since it was synthesized in a precursor form and processed, presumably by peptide cleavage, to a mature form; the maturation process was inhibited by addition of a proton ionophore. Proteins synthesized in minicells were localized as follows: FlaFVI was localized to the soluble fraction (cytoplasm); pre-FlaFVIII and FlaFVIII were localized to the particulate fraction (membrane or high-molecular-weight aggregate); FlaFV and FlaFVII were localized to both fractions. The significance of these locations in terms of known or suspected roles in the flagellar apparatus is discussed.Entities:
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Year: 1987 PMID: 3301807 PMCID: PMC212441 DOI: 10.1128/jb.169.8.3617-3624.1987
Source DB: PubMed Journal: J Bacteriol ISSN: 0021-9193 Impact factor: 3.490