Release of flagellar filament-hook-rod complex by a Salmonella typhimurium mutant defective in the M ring of the basal body

Okino, Hiroshi; Isomura, Mitsuo; Yamaguchi, Shigeru; Magariyama, Yukio; Kudo, Satoshi; Aizawa, Shin‐Ichi

doi:10.1128/jb.171.4.2075-2082.1989

Cited by 67 publications

(42 citation statements)

References 26 publications

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“…Purification and amino acid analysis of the B. subtilis hook Because the flagellar filaments are external to the cell, they tend to detach from the cell body by shear force, leaving the flagellar basal body in the membrane, as shown for S. typhimurium (Okino et al, 1989). This is also true for B. subtilis: pipetting the cell suspension effectively shears off most of the filaments.…”

Section: Resultsmentioning

confidence: 99%

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Kubori

Okumura

Kobayashi

et al. 1997

Molecular Microbiology

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SummaryThe flagellar hook-basal body (HBB) complex of the Gram-positive bacterium Bacillus subtilis was purified and analysed by electron microscopy, gel electrophoresis, and amino acid sequencing of the major component proteins. The purified HBB complex consisted of the inner (M and S) rings, a rod and a hook. There were no outer (P and L) rings that are found in Gram-negative bacteria. The hook was 15 nm in thickness and 70 nm in length, which is thinner and longer than the hook of Salmonella typhimurium. The hook protein had an apparent molecular mass of 29 kDa, and its N-terminal sequence was identical to that of B. subtilis FlgG

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Section: Resultsmentioning

confidence: 99%

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Kubori

Okumura

Kobayashi

et al. 1997

Molecular Microbiology

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“…propagated over considerable distances, since the length of the rod exceeds the direct reach of the P ring, which is located in the vicinity of the junction between the FlgG portion and the proximal portion (39,44). Independent evidence for propagated effects in the rod comes from a mutant whose rod is prone to shear at the junction between the proximal and distal zones (39), yet whose defect lies in the M-ring protein, which is located about 20 nm away.…”

mentioning

confidence: 99%

“…Independent evidence for propagated effects in the rod comes from a mutant whose rod is prone to shear at the junction between the proximal and distal zones (39), yet whose defect lies in the M-ring protein, which is located about 20 nm away.…”

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confidence: 99%

Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants

1990

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The process of flagellar assembly in Salmonella typhimurium was investigated by using temperature-sensitive mutants. The mutants were grown at the restrictive temperature and then at the permissive temperature, with radiolabel supplied in the first phase of the experiment and not the second, or vice versa. Flagellar hook-basal body complexes were then purified and analyzed by gel electrophoresis and autoradiography. The extent to which a given protein was labeled in the two phases of the experiment provided information as to whether it preceded or followed the block caused by the mutant protein. We conclude the following concerning flagellar assembly. The M-ring protein (FliF) is stably incorporated in the earliest stage detected, along with two previously unknown proteins, with apparent molecular masses of 23 and 26 kilodaltons, respectively, and possibly one of the switch components, FliG. Independent of that event and all other events, the P-ring and Lring proteins (FlgI and FlgH) are synthesized and exported to the periplasm and outer membrane by the primary cellular export pathway. Rod assembly occurs by export (via the flagellum-specific pathway) of subunits of four proteins, FlgB, FlgC, FlgF, and FlgG, and their incorporation, probably in that order, into the rod structure; this stage requires theflhA andfliI genes, perhaps because they encode part of the export apparatus. Once rod assembly is complete, the FlgI and FlgH proteins assemble around the rod to form the P and L rings. The rod structure, which is only metastable while it is being constructed, becomes stable upon Pring addition. Export (via the flagellum-specific pathway) and assembly of hook protein, hook-associated proteins, and filament protein then occur successively. A number of flagellar proteins, whose genetic origin and structural role are not yet known, were identified on the basis of their dependence on the flagellar master operon for expression.Bacterial flagella are complex organelles, whose structure spans the cell envelope and extends far beyond it and whose assembly therefore entails special logistical problems. An indication of the overall complexity of the flagellar system is the fact that in Salmonella typhimurium, for example, it is encoded by about 40 genes (22,35). The known structures of the flagellum (Fig. 1) are the basal body, the hook, the hook-filament junction zone, the filament, and the filament cap (11,14,23,24). Within the basal body, the morphology can be further broken down into the inner (M and S) rings, the rod, and the outer (P and L) rings (11). The genes and gene products responsible for most of these morphological features are known (1, 13, 16-19, 25, 26, 27, 31, 33, 39; M. Homma, K. Kutsukake, M. Hasebe, T. lino, and R. M. Macnab, J. Mol. Biol., in press). Among structures that have not yet been positively identified by electron microscopy, there is the flagellar switch, which is responsible for determining the direction of flagellar rotation (15, 29, 51, 52), and structure associated with two motility p...

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“…Okino et al (5) observed that highly viscous medium destabilizes the flagella of Salmonella typhimurium. They analyzed a particular mutant strain that swims well in liquid, but loses its flagella in semi-solid agar or liquid media with high viscosity.…”

Section: Discussionmentioning

confidence: 99%

Characterization of Pseudomonas paucimobilis FP2001 Which Forms Flagella Depending upon the Presence of Rhamnose in Liquid Medium

Miake

Murata

Kuroiwa

et al. 1995

Microbiology and Immunology

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Release of flagellar filament-hook-rod complex by a Salmonella typhimurium mutant defective in the M ring of the basal body

Cited by 67 publications

References 26 publications

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Purification and characterization of the flagellar hook–basal body complex of Bacillus subtilis

Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants

Characterization of Pseudomonas paucimobilis FP2001 Which Forms Flagella Depending upon the Presence of Rhamnose in Liquid Medium

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