Mechanisms and Dynamics of the Bacterial Flagellar Motor

Nord, Ashley L.; Pedaci, Francesco

doi:10.1007/978-3-030-46886-6_5

Cited by 9 publications

(5 citation statements)

References 170 publications

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“…Our measurements were based on a modification of the BFM bead assay, typically used to study the dynamics of the motor ( 29 , 40 ). We measured the BFM angular speed via bright-field microscopy [with up to a 20-kHz sampling rate; ( 41 )] by tracking the recorded holograms of the off-axis rotation of 600-nm-diameter beads attached to flagellar stubs of individual immobilized E. coli cells (see Fig.…”

Section: Resultsmentioning

confidence: 99%

“…1, C to E ). We note that the number of the active stator units in the motor is dynamic, mechanosensitive, and PMF dependent ( 29 , 34 , 42 , 43 ). By tuning the laser pulse duration and the time between pulses, we aimed to avoid an increase in the time-averaged PMF and thus avoid an increase in stator number.…”

Section: Resultsmentioning

confidence: 99%

“…In this work, we turn to a biological probe to characterize the spatiotemporal PMF dynamics on single E. coli cells. The bacterial flagellar motor (BFM) is the PMF-driven nano-rotary motor located at the base of each flagellum, which drives cell motility in many motile bacteria ( 26 , 28 , 29 ). We use spatiotemporally structured laser excitation on single bacteria expressing the light-driven proton pump proteorhodopsin (PR) to controllably augment the PMF in space and time.…”

Section: Introductionmentioning

confidence: 99%

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Spatiotemporal dynamics of the proton motive force on single bacterial cells

Biquet-Bisquert,

Carrio,

Meyer

et al. 2024

Sci. Adv.

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Electrochemical gradients across biological membranes are vital for cellular bioenergetics. In bacteria, the proton motive force (PMF) drives essential processes like adenosine triphosphate production and motility. Traditionally viewed as temporally and spatially stable, recent research reveals a dynamic PMF behavior at both single-cell and community levels. Moreover, the observed lateral segregation of respiratory complexes could suggest a spatial heterogeneity of the PMF. Using a light-activated proton pump and detecting the activity of the bacterial flagellar motor, we perturb and probe the PMF of single cells. Spatially homogeneous PMF perturbations reveal millisecond-scale temporal dynamics and an asymmetrical capacitive response. Localized perturbations show a rapid lateral PMF homogenization, faster than proton diffusion, akin to the electrotonic potential spread observed in passive neurons, explained by cable theory. These observations imply a global coupling between PMF sources and consumers along the membrane, precluding sustained PMF spatial heterogeneity but allowing for rapid temporal changes.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Spatiotemporal dynamics of the proton motive force on single bacterial cells

Biquet-Bisquert,

Carrio,

Meyer

et al. 2024

Sci. Adv.

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“…The flagellar T3SS is located at the base of the flagellum and it is one of the earliest structures of the assembly, together with the MS ring of the basal body. The structure and mechanism behind basal body function were a subject of several recent reviews [ 9 , 10 , 11 , 12 ], and they will not be considered further here. Instead, we will focus on the various aspects of the flagellar filament, its components and the role it plays in host–pathogen interactions.…”

Section: Introductionmentioning

confidence: 99%

Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure

Nedeljković

Sastre

Sundberg

2021

IJMS

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The bacterial flagellum is a complex and dynamic nanomachine that propels bacteria through liquids. It consists of a basal body, a hook, and a long filament. The flagellar filament is composed of thousands of copies of the protein flagellin (FliC) arranged helically and ending with a filament cap composed of an oligomer of the protein FliD. The overall structure of the filament core is preserved across bacterial species, while the outer domains exhibit high variability, and in some cases are even completely absent. Flagellar assembly is a complex and energetically costly process triggered by environmental stimuli and, accordingly, highly regulated on transcriptional, translational and post-translational levels. Apart from its role in locomotion, the filament is critically important in several other aspects of bacterial survival, reproduction and pathogenicity, such as adhesion to surfaces, secretion of virulence factors and formation of biofilms. Additionally, due to its ability to provoke potent immune responses, flagellins have a role as adjuvants in vaccine development. In this review, we summarize the latest knowledge on the structure of flagellins, capping proteins and filaments, as well as their regulation and role during the colonization and infection of the host.

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“…It has been shown that the plug region of PomB prevents the ion influx by blocking the rotation of the rotor as a spanner to interact with the periplasmic loops of PomA (Homma et al, 2021). Once the stator unit is incorporated into the rotor, the interaction between FliG and stator units promotes stator-peptidoglycan binding, completing the assembly (Terahara et al, 2017;Kojima et al, 2018;Nord and Pedaci, 2020). A simple Hill-Langmuir absorption model has been proposed to describe the dynamic response of stator unit to the change of external load (Nord et al, 2017a;Wadhwa et al, 2019).…”

Section: Introductionmentioning

confidence: 99%

Stator Dynamics Depending on Sodium Concentration in Sodium-Driven Bacterial Flagellar Motors

et al. 2021

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Bacterial flagellar motor (BFM) is a large membrane-spanning molecular rotary machine for swimming motility. Torque is generated by the interaction between the rotor and multiple stator units powered by ion-motive force (IMF). The number of bound stator units is dynamically changed in response to the external load and the IMF. However, the detailed dynamics of stator unit exchange process remains unclear. Here, we directly measured the speed changes of sodium-driven chimeric BFMs under fast perfusion of different sodium concentration conditions using computer-controlled, high-throughput microfluidic devices. We found the sodium-driven chimeric BFMs maintained constant speed over a wide range of sodium concentrations by adjusting stator units in compensation to the sodium-motive force (SMF) changes. The BFM has the maximum number of stator units and is most stable at 5 mM sodium concentration rather than higher sodium concentration. Upon rapid exchange from high to low sodium concentration, the number of functional stator units shows a rapidly excessive reduction and then resurrection that is different from predictions of simple absorption model. This may imply the existence of a metastable hidden state of the stator unit during the sudden loss of sodium ions.

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Mechanisms and Dynamics of the Bacterial Flagellar Motor

Cited by 9 publications

References 170 publications

Spatiotemporal dynamics of the proton motive force on single bacterial cells

Spatiotemporal dynamics of the proton motive force on single bacterial cells

Bacterial Flagellar Filament: A Supramolecular Multifunctional Nanostructure

Stator Dynamics Depending on Sodium Concentration in Sodium-Driven Bacterial Flagellar Motors

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