Motility Protein Complexes in the Bacterial Flagellar Motor

Tang, Hua; Braun, Timothy F.; Blair, David F.

doi:10.1006/jmbi.1996.0453

Cited by 120 publications

(160 citation statements)

References 28 publications

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“…FliM-binding Surfaces on FliN-FliN was shown to bind specifically to FliM C in studies that used either GST pulldown assays (44) or blot overlay assays (46). Those studies predate the FliN crystal structure, and the regions on FliN that bind to FliM C were not mapped.…”

Section: Resultsmentioning

confidence: 99%

“…Co-pelleting Assay for Protein Binding-Glutathione S-transferase (GST) pulldown experiments were carried out essentially as described (33,44) with minor modifications. The experiments used a ⌬flhDC strain that expresses no chromosomal flagellar genes and a "two-cell" protocol in which GST-FliM and FliN (wild-type or mutant) were expressed in separate cells.…”

Section: Methodsmentioning

confidence: 99%

“…The experiments used a ⌬flhDC strain that expresses no chromosomal flagellar genes and a "two-cell" protocol in which GST-FliM and FliN (wild-type or mutant) were expressed in separate cells. Control experiments used GST only in place of the GST-FliM fusion, expressed from plasmid pHT100 (44). Cells were cultured overnight at 32°C in 40 ml of LB medium with appropriate antibiotics and 400 M IPTG.…”

Section: Methodsmentioning

confidence: 99%

“…The supernatant was removed, and GST-FliM and associated proteins were released from the beads by addition of 50 l of elution buffer (50 mM reduced glutathione in 50 mM Tris-HCl, pH 8) for 10 min at room temperature with gentle rotation. Beads were pelleted, and the supernatant was collected for analysis by SDS-PAGE and immunoblotting using anti-FliN antibody as described (36,44).…”

Section: Methodsmentioning

confidence: 99%

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Subunit Organization and Reversal-associated Movements in the Flagellar Switch of Escherichia coli

Sarkar

Paul

Blair

2010

Journal of Biological Chemistry

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Bacterial flagella contain a rotor-mounted protein complex termed the switch complex that functions in flagellar assembly, rotation, and clockwise/counterclockwise direction control. In Escherichia coli and Salmonella, the switch complex contains the proteins FliG, FliM, and FliN and corresponds structurally with the C-ring in the flagellar basal body. Certain features of subunit organization in the switch complex have been deduced previously, but details of subunit organization in the lower part of the C-ring and the molecular movements responsible for motor switching remain unclear. In this study, we use crosslinking, binding, and mutational experiments to examine subunit organization in the bottom of the C-ring and to probe movements that occur upon switching. The results show that FliN tetramers alternate with FliM C-terminal domains to form the bottom of the C-ring in an arrangement that closely reproduces the major features observed in electron microscopic reconstructions. When motors were switched to clockwise rotation by a repellent stimulus, cross-link yields were altered in a pattern indicating relative movement of FliN and FliM C . These results are discussed in the framework of a structurally grounded hypothesis for the switching mechanism.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Subunit Organization and Reversal-associated Movements in the Flagellar Switch of Escherichia coli

Sarkar

Paul

Blair

2010

Journal of Biological Chemistry

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“…MotB is believed to act as an anchor to the cell wall (11,12) and to work with MotA as the stator of the flagellar motor. It has been shown that MotA interacts, but only weakly, with FliG and FliM of the switch complex (49).…”

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confidence: 99%

Putative channel components for the fast-rotating sodium-driven flagellar motor of a marine bacterium

et al. 1997

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The polar flagellum of Vibrio alginolyticus rotates remarkably fast (up to 1,700 revolutions per second) by using a motor driven by sodium ions. Two genes, motX and motY, for the sodium-driven flagellar motor have been identified in marine bacteria, Vibrio parahaemolyticus and V. alginolyticus. They have no similarity to the genes for proton-driven motors, motA and motB, whose products constitute a proton channel. MotX was proposed to be a component of a sodium channel. Here we identified additional sodium motor genes, pomA and pomB, in V. alginolyticus. Unexpectedly, PomA and PomB have similarities to MotA and MotB, respectively, especially in the predicted transmembrane regions. These results suggest that PomA and PomB may be sodium-conducting channel components of the sodium-driven motor and that the motor part consists of the products of at least four genes, pomA, pomB, motX, and motY. Furthermore, swimming speed was controlled by the expression level of the pomA gene, suggesting that newly synthesized PomA proteins, which are components of a force-generating unit, were successively integrated into the defective motor complexes. These findings imply that Na ؉ -driven flagellar motors may have similar structure and function as proton-driven motors, but with some interesting differences as well, and it is possible to compare and study the coupling mechanisms of the sodium and proton ion flux for the force generation.

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Comparison of Escherichia coli Responses to Different Silver Nanoparticles with Different Particle Sizes and Surface Coatings

Liu,

Sun,

Zhang

et al. 2024

Part & Part Syst Charact

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AgNPs are widely used for their excellent antimicrobial properties, whereas the cytotoxicity they possess makes them an unignorable environmental problem. Considering the impact of particle size and surface coating on the antibacterial properties, four types of AgNPs are selected: citrate‐coated 20 nm (C20), polyvinylpyrrolidone‐coated 20 nm (P20), citrate‐coated 100 nm (C100), and polyvinylpyrrolidone‐coated 100 nm (P100) AgNPs. All four AgNPs significantly affect the ribosome pathway, with stronger binding of large and small subunits. 20 nm and 100 nm AgNPs both affected the biosynthesis and metabolism of several amino acids (including arginine, glycine, serine, threonine, glyoxylic acid, and dicarboxylic acid). P20 and C100 exposure affected bacterial chemotaxis and flagellar motility. This study preliminarily explained the response mechanism of E. coli to AgNPs with different properties, which provided a theoretical basis for predicting the response mechanism of E. coli to metal nanoparticles with similar properties.

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Motility Protein Complexes in the Bacterial Flagellar Motor

Cited by 120 publications

References 28 publications

Subunit Organization and Reversal-associated Movements in the Flagellar Switch of Escherichia coli

Subunit Organization and Reversal-associated Movements in the Flagellar Switch of Escherichia coli

Putative channel components for the fast-rotating sodium-driven flagellar motor of a marine bacterium

Comparison of Escherichia coli Responses to Different Silver Nanoparticles with Different Particle Sizes and Surface Coatings

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