Geometry of the Flagellar Motor in the Cytoplasmic Membrane of as Determined by Stereo-photogrammetry of Quick-freeze Deep-etch Replica Images

Katayama, Eisaku; Shiraishi, T; Oosawa, Kenji; Baba, Norio; Aizawa, Shin‐Ichi

doi:10.1006/jmbi.1996.0038

Cited by 84 publications

(67 citation statements)

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“…Ultrastructural studies of basal bodies are consistent with the hypothesis Electron microscopic studies indicate that, when the MS ring protein (FliF) is overproduced, it assembles spontaneously into MS rings, which have a central pore with a diameter of slightly under 10 nm (Katayama et al, 1996). It cannot be an aqueous pore, as the cell survives large numbers of MS rings in its membrane.…”

Section: Flip and Flir Are Associated With The Flagellar Basal Bodysupporting

confidence: 62%

“…En face images of basal bodies viewed from the cytoplasmic side show the cylindrical structure known as the C ring, which is believed to be the rotor element of the motor switch. Inside the cylinder, on axis, is a knob-like protrusion, which might very well correspond to the export apparatus (Katayama et al, 1996).…”

Section: Flip and Flir Are Associated With The Flagellar Basal Bodymentioning

confidence: 99%

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The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body

Fan

Ohnishi

Francis

et al. 1997

Molecular Microbiology

120

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SummaryMost of the structural components of the flagellum of Salmonella typhimurium are exported through a flagellum-specific pathway, which is a member of the family of type III secretory pathways. The export apparatus for this process is poorly understood. A previous study has shown that two proteins, about 23 and 26 kDa in size and of unknown genetic origin, are incorporated into the flagellar basal body at a very early stage of flagellar assembly. In the present study, we demonstrate that these basal body proteins are FliP (in its mature form after signal peptide cleavage) and FliR respectively. Both of these proteins have homologues in other type III secretion systems. By placing a FLAG epitope tag on FliR and the MS-ring protein FliF and immunoblotting isolated hook basal body complexes with anti-FLAG monoclonal antibody, we estimate (using the FLAG-tagged FliF as an internal reference) that the stoichiometry of FliR is fewer than three copies per basal body. An independent estimate of stoichiometry was made using data from an earlier quantitative radiolabelling analysis, yielding values of around four or five subunits per basal body for FliP and around one subunit per basal body for FliR. Immunoelectron microscopy using anti-FLAG antibody and gold-protein A suggests that FliR is located near the MS ring. We propose that the flagellar export apparatus contains FliP and FliR and that this apparatus is embedded in a patch of membrane in the central pore of the MS ring.

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Section: Flip and Flir Are Associated With The Flagellar Basal Bodysupporting

confidence: 62%

Section: Flip and Flir Are Associated With The Flagellar Basal Bodymentioning

confidence: 99%

The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body

Fan

Ohnishi

Francis

et al. 1997

Molecular Microbiology

120

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“…A small dome with a dip found in the C ring, C rod, is a good candidate for the export apparatus (Katayama et al 1996).…”

Section: Flagellar Structurementioning

confidence: 99%

Bacterial flagellation and cell division

Aizawa

Kubori

1998

Genes to Cells

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The peritrichous flagella of Salmonella are synthesized and function through many cell generations. There are two different aspects in the relationship between flagellar biogenesis and cell division. Filament growth is independent from the cell cycle and the length of filaments appear to be locally controlled at each flagellar base, whereas the number of filaments (or flagellar basal bodies) is dependent on cell cycle. We present a model to explain how the number of filaments is maintained through generations. We will also introduce a new direction for research that might directly connect flagellation and cell division; the global communication between flagellar genes and external factors of a complex regulatory network in a cell.

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“…The analysis of the basal-body structure of S. typhimurium was almost finished by 1991 when the S ring, one of the inner rings and a long-time-elusive component, were identified as a part of a multidomain complex (now called the MS ring complex) consisting of a single protein, FliF (Ueno et al, 1992;. Recent efforts have focused on the structural study of the fragile components, which are weakly bound to the basal body (Khan et al, 1992;Francis et al, 1994;Katayama et al, 1996).…”

Section: Introductionmentioning

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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Geometry of the Flagellar Motor in the Cytoplasmic Membrane of as Determined by Stereo-photogrammetry of Quick-freeze Deep-etch Replica Images

Cited by 84 publications

References 0 publications

The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body

The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal body

Bacterial flagellation and cell division

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

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