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Flagellar Motor sentence examples within chemotaxis signaling protein

chemotaxis signaling protein

The change in rotation is triggered by the binding of the chemotaxis signaling protein CheY-Phosphate (CheY-P) to the C-ring in the flagellar motor.

ZomB is essential for chemotaxis of Vibrio alginolyticus by the rotational direction control of the polar flagellar motor.

chemotaxis signaling protein

The change in rotation is triggered by the binding of the chemotaxis signaling protein CheY to the C-ring in the flagellar motor.

ZomB is essential for chemotaxis of Vibrio alginolyticus by the rotational direction control of the polar flagellar motor

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Flagellar Motor sentence examples within Bacterial Flagellar Motor

Bacterial Flagellar Motor

The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key determinant of pathogenicity.

Structural basis of assembly and torque transmission of the bacterial flagellar motor

Bacterial Flagellar Motor

This rotation is driven by a membrane protein known as the stator-complex, which drives the rotor of the bacterial flagellar motor.

Separation and enrichment of sodium-motile bacteria using cost-effective microfluidics.

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Flagellar Motor sentence examples within Bidirectional Flagellar Motor

Bidirectional Flagellar Motor

The bidirectional flagellar motor of the bacterium Escherichia coli recruits or releases torque-generating units (stator units) in response to changes in load.

Mechanosensitive remodeling of the bacterial flagellar motor is independent of direction of rotation

Bidirectional Flagellar Motor

Motility in many bacteria is powered by a bidirectional flagellar motor.

Multiple CheY Homologs Control Swimming Reversals and Transient Pauses in Azospirillum brasilense.

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Flagellar Motor sentence examples within flagellar motor protein

flagellar motor protein

Sequencing and gene annotation results evidently showed presence of chemotaxis genes and flagellar motor proteins in Bacillus subtilis draft genome.

Annotation of chemotaxis gene clusters and proteins involved in chemotaxis of Bacillus subtilis strain MB378 capable of biodecolorizing different dyes

flagellar motor protein

In the chemotaxis of Escherichia coli, the cell’s behavioral switch involves binding of the phosphorylated form of the chemotaxis signaling protein CheY (CheYp) to the flagellar motor protein FliM, which induces the motor to rotate clockwise; otherwise, the motor rotates counterclockwise.

High pressure inhibits signaling protein binding to the flagellar motor and bacterial chemotaxis through enhanced hydration

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Flagellar Motor sentence examples within flagellar motor switch

flagellar motor switch

RT-PCR showed differential expression of treS (trehalose synthase), rpoS (sigma factor), mucA (alginate regulatory gene), and fliM (flagellar motor switch protein gene) in response to exposure to RH10%.

Drought tolerant Pseudomonas sp. showed differential expression of stress-responsive genes and induced drought tolerance in Arabidopsis thaliana.

flagellar motor switch

In addition, flagellar motor switch FliG gene silencing resulted in reduced bacterial motility.

Gene silencing based on RNA-guided catalytically inactive Cas9 (dCas9): a new tool for genetic engineering in Leptospira

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Flagellar Motor sentence examples within flagellar motor torque

flagellar motor torque

A supercritical Hopf bifurcation in the flagellar orientation beyond a critical ratio of flagellar motor torque to hook bending stiffness, which is set by the spontaneous curvature of the flexible hook, the shape of the cell body, and the flagellum geometry, can have a dramatic effect on the cell’s trajectory through the fluid.

Helical trajectories of swimming cells with a flexible flagellar hook

flagellar motor torque

cholerae flagellar motor torque, and consequently, mucus penetration.

Acidic pH reduces Vibrio cholerae motility in mucus by weakening flagellar motor torque

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Flagellar Motor sentence examples within flagellar motor require

flagellar motor require

The self‐assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio‐temporal synchronization of gene expression with proper protein localization and association of dozens of protein components.

In situ imaging of the bacterial flagellar motor disassembly and assembly processes

flagellar motor require

The self-assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio-temporal synchronization of gene expression with proper protein localization and association of dozens of protein components.

In situ imaging of the bacterial flagellar motor disassembly and assembly processes.

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Flagellar Motor sentence examples within flagellar motor depend

flagellar motor depend

Behavior of the bacterial flagellar motor depends sensitively on the external loads it drives.

Dynamics of switching at stall reveals nonequilibrium mechanism in the allosteric regulation of the bacterial flagellar switch

flagellar motor depend

We measure how the assembly of the bacterial flagellar motor depends on its operational parameters, such as speed and torque.

Torque-dependent remodeling of the bacterial flagellar motor

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Flagellar Motor sentence examples within flagellar motor significantly

flagellar motor significantly

Disruption of the flagellar motor significantly decreases host mortality of V.

The Polar Flagellar Transcriptional Regulatory Network in Vibrio campbellii Deviates from Canonical Vibrio Species

flagellar motor significantly

campbellii pathogenesis, and disruption of the flagellar motor significantly decreases host mortality.

The polar flagellar transcriptional regulatory network in Vibrio campbellii deviates from canonical Vibrio species

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10.1007/978-3-030-58971-4_8

The flagellar motor, which structurally resembles an artificial motor, is embedded within the cell envelop and spins at several hundred revolutions per second.

Architecture and Assembly of the Bacterial Flagellar Motor Complex.

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10.1101/2021.08.23.457452

Our high-resolution in-situ structures reveal that the multi-protein collar has a remarkable structural plasticity essential not only for assembly of flagellar motors in the highly curved membrane of spirochetes but also for generation of the high torque necessary for spirochete motility.

Characterization of the flagellar collar reveals structural plasticity essential for spirochete motility

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10.1128/JB.00320-21

Putative Spanner Function of the Vibrio PomB Plug Region in the Stator Rotation Model for the Flagellar Motor The bacterial flagellar motor is a biological machine driven by ion flow.

Article of Significant Interest in This Issue

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10.1101/2021.02.11.430483

Mutant cells, which were rendered non-motile due to the absence of the PTS (phosphotransferase system) sugar uptake mechanism, exhibited motility when exposed to the non-metabolisable attractant confirming that mere sensing can induce torque in flagellar motor.

Effect of ligand sensing on flagellar bundle formation in bacteria

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10.1128/mBio.02392-21

The FliE protein plays dual roles in the assembly of the Salmonella flagellum as the final component of the flagellar type III secretion system (fT3SS) and as an adaptor protein that anchors the rod (drive shaft) of the flagellar motor to the membrane-imbedded MS-ring structure.

Genetic Analysis of the Salmonella FliE Protein That Forms the Base of the Flagellar Axial Structure

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10.1038/s41467-021-24507-9

The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly.

Native flagellar MS ring is formed by 34 subunits with 23-fold and 11-fold subsymmetries

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10.1016/j.bpj.2021.04.033

If a cell senses that the concentration of an attractant has increased, their flagellar motors decrease the switching frequency from counterclockwise to clockwise direction of rotation, which causes a longer run in swimming up the concentration gradient than swimming down.

Biased re-orientation in the chemotaxis of peritrichous bacteria Salmonella enterica serovar Typhimurium.

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10.7554/eLife.62848

It is well known that flagellated bacteria, such as Escherichia coli, sense chemicals in their environment by a chemoreceptor and relay the signals via a well-characterized signaling pathway to the flagellar motor.

Ligand sensing enhances bacterial flagellar motor output via stator recruitment

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10.1073/pnas.2105566118

aeruginosa uses a diguanylate cyclase, via a complex web of protein–protein interactions, to integrate signaling through the T4P and the flagellar motor to fine-tune c-di-GMP levels.

Interaction between the type 4 pili machinery and a diguanylate cyclase fine-tune c-di-GMP levels during early biofilm formation

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10.1038/s41467-020-20558-6

Methyl-accepting chemotaxis proteins (MCPs) detect specific ligands and control the direction of the flagellar motor, promoting tumbling and changes in direction (if a repellent is detected) or smooth swimming (in the presence of an attractant).

Regulatory protein HilD stimulates Salmonella Typhimurium invasiveness by promoting smooth swimming via the methyl-accepting chemotaxis protein McpC

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10.3389/fmicb.2021.668892

A number of bacterial species control the function of the flagellar motor in response to the levels of the secondary messenger c-di-GMP, which is often mediated by c-di-GMP-binding proteins that act as molecular brakes or clutches to slow the motor rotation.

The Stand-Alone PilZ-Domain Protein MotL Specifically Regulates the Activity of the Secondary Lateral Flagellar System in Shewanella putrefaciens

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10.1101/2021.07.06.451194

GFP labeling showed the localization of the photoresponsive enzyme at the cell poles where flagellar motors reside.

Light-dependent synthesis of a nucleotide second messenger controls bacterial motility

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10.1101/2021.03.16.435749

We focused on the Vibrio PomB plug region, which has been reported to control the activation of flagellar motors.

Function of the Vibrio PomB plug region based on the stator rotation model for bacterial flagellar motor

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10.3389/fmicb.2021.664826

This behavior is mediated by dedicated signal transduction pathways that couple environment sensing with changes in the direction of rotation of flagellar motors to ultimately affect the motility pattern.

Multiple CheY Proteins Control Surface-Associated Lifestyles of Azospirillum brasilense

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10.1016/j.csbj.2019.07.020

The signal transducers transmit environmental signals to the flagellar motor through a cytoplasmic chemotactic signaling pathway.

Directional Switching Mechanism of the Bacterial Flagellar Motor

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10.1088/1751-8121/ab5425

Bacteria such as {\it Escherichia coli} move about in a series of runs and tumbles: while a run state (straight motion) entails all the flagellar motors spinning in counterclockwise (CCW) mode, a tumble is caused by a shift in the state of one or more motors to clockwise (CW) spinning.

A path-integral characterization of run and tumble motion and chemotaxis of bacteria

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10.1017/JFM.2018.799

Single-flagellated bacteria propel themselves by rotating a flagellar motor, translating rotation to the filament through a compliant hook and subsequently driving the rotation of the flagellum.

Locomotion of a single-flagellated bacterium

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10.1136/bcr-2019-232785

We conclude that the 65-kDa protein is a component--probably the main component--of this important substructure of the flagellar motor.

Severe flagellate erythema in idiopathic dermatomyositis

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10.1016/j.jmb.2019.08.001

Fumarate, an electron acceptor in anaerobic respiration of Escherichia coli, has an additional function of assisting the flagellar motor to shift from counterclockwise to clockwise rotation, with a consequent modulation of the bacterial swimming behavior.

A mechanism of modulating the direction of flagellar rotation in bacteria by fumarate and fumarate reductase.

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10.2210/PDB6AHQ/PDB

FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria.

Structure of Vibrio FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function.

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10.1128/mBio.00292-19

FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria.

Structure of Vibrio FliL, a New Stomatin-like Protein That Assists the Bacterial Flagellar Motor Function

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10.1128/mBio.01732-19

Species-specific adaptations to flagellar motors impact stator function to meet the demands of each species to sufficiently power flagellar rotation.

A Chaperone for the Stator Units of a Bacterial Flagellum

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10.1128/JB.00439-19

Cryo-electron tomography continues to provide new insights into the structure and function of chemosensory receptors and flagellar motors, while advances in protein labeling and tracking are applied to understand information flow between receptor and motor.

New Twists and Turns in Bacterial Locomotion and Signal Transduction.

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10.1093/bioinformatics/btz053

Examples of complex molecular systems include protein structures such as the F1Fo-ATPase, the ribosome, or the flagellar motor: each one of these structures requires most or all of its components to function properly.

Tracing the ancestry of operons in bacteria

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10.3390/biom9070279

Despite structural diversity of the flagella among bacterial species, flagellated bacteria share a common rotary nanomachine, namely the flagellar motor, which is located at the base of the filament.

Flagella-Driven Motility of Bacteria

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10.1128/mBio.01237-19

Here we used the model organism Caulobacter crescentus to demonstrate that polar pili are highly dynamic structures that are functionally interconnected with the flagellar motor to mediate surface sensing, thereby enforcing rapid and permanent surface attachment.

Tad Pili Play a Dynamic Role in Caulobacter crescentus Surface Colonization

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10.1074/jbc.RA119.009739

As an effector of c-di-GMP in Escherichia coli and related species, the PilZ domain–containing protein YcgR responds to elevated c-di-GMP concentrations and acts on the flagellar motor to suppress bacterial motility in a brakelike fashion, which promotes bacterial surface attachment.

Structural insights into the mechanism of c-di-GMP–bound YcgR regulating flagellar motility in Escherichia coli

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10.1101/2019.12.26.888701

jejuni’s flagella deviate from the Enterobacteriaceael norm in other ways: their flagellar motors produce much higher torque and their flagellar filament is made of two different zones of two different flagellins.

“Campylobacter jejuni motility integrates specialized cell shape, flagellar filament, and motor, to coordinate action of its opposed flagella in viscous media”

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10.1101/567438

We provide evidence that the second messenger cAMP is the likely signal generated by flagellar-mediated surface attachment and show that cAMP is sufficient to alter the behavior of the flagellar motor.

Modulation of Flagellar Rotation in Surface-Attached Bacteria: A Circuit for Rapid Surface-Sensing

Flagellar Motor
Encyclopedia

What is/are Flagellar Motor?

Flagellar Motor - The flagellar motor, which structurally resembles an artificial motor, is embedded within the cell envelop and spins at several hundred revolutions per second. [1] Our high-resolution in-situ structures reveal that the multi-protein collar has a remarkable structural plasticity essential not only for assembly of flagellar motors in the highly curved membrane of spirochetes but also for generation of the high torque necessary for spirochete motility. [2] Putative Spanner Function of the Vibrio PomB Plug Region in the Stator Rotation Model for the Flagellar Motor The bacterial flagellar motor is a biological machine driven by ion flow. [3] Mutant cells, which were rendered non-motile due to the absence of the PTS (phosphotransferase system) sugar uptake mechanism, exhibited motility when exposed to the non-metabolisable attractant confirming that mere sensing can induce torque in flagellar motor. [4] The FliE protein plays dual roles in the assembly of the Salmonella flagellum as the final component of the flagellar type III secretion system (fT3SS) and as an adaptor protein that anchors the rod (drive shaft) of the flagellar motor to the membrane-imbedded MS-ring structure. [5] The bacterial flagellar MS ring is a transmembrane complex acting as the core of the flagellar motor and template for flagellar assembly. [6] If a cell senses that the concentration of an attractant has increased, their flagellar motors decrease the switching frequency from counterclockwise to clockwise direction of rotation, which causes a longer run in swimming up the concentration gradient than swimming down. [7] It is well known that flagellated bacteria, such as Escherichia coli, sense chemicals in their environment by a chemoreceptor and relay the signals via a well-characterized signaling pathway to the flagellar motor. [8] aeruginosa uses a diguanylate cyclase, via a complex web of protein–protein interactions, to integrate signaling through the T4P and the flagellar motor to fine-tune c-di-GMP levels. [9] Methyl-accepting chemotaxis proteins (MCPs) detect specific ligands and control the direction of the flagellar motor, promoting tumbling and changes in direction (if a repellent is detected) or smooth swimming (in the presence of an attractant). [10] A number of bacterial species control the function of the flagellar motor in response to the levels of the secondary messenger c-di-GMP, which is often mediated by c-di-GMP-binding proteins that act as molecular brakes or clutches to slow the motor rotation. [11] GFP labeling showed the localization of the photoresponsive enzyme at the cell poles where flagellar motors reside. [12] We focused on the Vibrio PomB plug region, which has been reported to control the activation of flagellar motors. [13] This behavior is mediated by dedicated signal transduction pathways that couple environment sensing with changes in the direction of rotation of flagellar motors to ultimately affect the motility pattern. [14] The signal transducers transmit environmental signals to the flagellar motor through a cytoplasmic chemotactic signaling pathway. [15] Bacteria such as {\it Escherichia coli} move about in a series of runs and tumbles: while a run state (straight motion) entails all the flagellar motors spinning in counterclockwise (CCW) mode, a tumble is caused by a shift in the state of one or more motors to clockwise (CW) spinning. [16] Single-flagellated bacteria propel themselves by rotating a flagellar motor, translating rotation to the filament through a compliant hook and subsequently driving the rotation of the flagellum. [17] We conclude that the 65-kDa protein is a component--probably the main component--of this important substructure of the flagellar motor. [18] Fumarate, an electron acceptor in anaerobic respiration of Escherichia coli, has an additional function of assisting the flagellar motor to shift from counterclockwise to clockwise rotation, with a consequent modulation of the bacterial swimming behavior. [19] FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. [20] FliL, a component protein of the flagellar motor, is known to enhance the motor performance under high-load conditions in some bacteria. [21] Species-specific adaptations to flagellar motors impact stator function to meet the demands of each species to sufficiently power flagellar rotation. [22] Cryo-electron tomography continues to provide new insights into the structure and function of chemosensory receptors and flagellar motors, while advances in protein labeling and tracking are applied to understand information flow between receptor and motor. [23] Examples of complex molecular systems include protein structures such as the F1Fo-ATPase, the ribosome, or the flagellar motor: each one of these structures requires most or all of its components to function properly. [24] Despite structural diversity of the flagella among bacterial species, flagellated bacteria share a common rotary nanomachine, namely the flagellar motor, which is located at the base of the filament. [25] Here we used the model organism Caulobacter crescentus to demonstrate that polar pili are highly dynamic structures that are functionally interconnected with the flagellar motor to mediate surface sensing, thereby enforcing rapid and permanent surface attachment. [26] As an effector of c-di-GMP in Escherichia coli and related species, the PilZ domain–containing protein YcgR responds to elevated c-di-GMP concentrations and acts on the flagellar motor to suppress bacterial motility in a brakelike fashion, which promotes bacterial surface attachment. [27] jejuni’s flagella deviate from the Enterobacteriaceael norm in other ways: their flagellar motors produce much higher torque and their flagellar filament is made of two different zones of two different flagellins. [28] We provide evidence that the second messenger cAMP is the likely signal generated by flagellar-mediated surface attachment and show that cAMP is sufficient to alter the behavior of the flagellar motor. [29]

chemotaxis signaling protein

The change in rotation is triggered by the binding of the chemotaxis signaling protein CheY-Phosphate (CheY-P) to the C-ring in the flagellar motor. [1] The change in rotation is triggered by the binding of the chemotaxis signaling protein CheY to the C-ring in the flagellar motor. [2]

Bacterial Flagellar Motor

The bacterial flagellar motor is a supramolecular protein machine that drives rotation of the flagellum for motility, which is essential for bacterial survival in different environments and a key determinant of pathogenicity. [1] This rotation is driven by a membrane protein known as the stator-complex, which drives the rotor of the bacterial flagellar motor. [2] Reversible switching of the bacterial flagellar motor between clockwise (CW) and counterclockwise (CCW) rotation is necessary for chemotaxis, which enables cells to swim towards favorable chemical habitats. [3] In most species, the rotation of the flagellum, driven by the Bacterial Flagellar Motor (BFM), is powered by H+ or Na+ ion transit through the torque-generating stator subunits of the motor complex. [4] The canonical chemotaxis network modulates the bias for a particular direction of rotation in the bacterial flagellar motor to help the cell migrate toward favorable chemical environments. [5] We report evidence further supporting homology between proteins in the F1FO‐ATP synthetase and the bacterial flagellar motor (BFM). [6] The bacterial flagellar motor tunes the assembly of its torque-generating stator complex with changes in external load. [7] The bacterial flagellar motor (BFM) is a protein complex that confers motility to cells and contributes to survival and virulence. [8] Detailed study of the micro and even nanolevel assembly of microbial life also intrigued biologists and engineers to generate molecular motors that mimic bacterial flagellar motor. [9] This study directly demonstrates the nature of the stator-rotor interaction and suggests how stator units assemble around the rotor and generate torque in the bacterial flagellar motor. [10] Evidence of homology between proteins in the ATP synthetase and the bacterial flagellar motor (BFM) has been accumulating since the 1980s. [11] Uniquely among them, the switch of the bacterial flagellar motor is not an on/off switch but rather controls the motor’s direction of rotation in response to binding of the signaling protein CheY. [12] The bacterial flagellar motor, a remarkable rotary machine, can rapidly switch between counterclockwise (CCW) and clockwise (CW) rotational directions to control the migration behavior of the bacterial cell. [13] The bacterial flagellar motor is a complex macromolecular machine whose function and self-assembly present a fascinating puzzle for structural biologists. [14] The bacterial flagellar motor implements autonomous torque regulation based on the stator’s dynamic structure; the stator units bind to and dissociate from the motor dynamically in response to environmental changes. [15] This study aimed to develop a propulsion design concept for smart drones (UAVs - Unmanned Aerial Vehicles) mimicking bacterial flagellar motor that can be found in many bacterial cells. [16] The bacterial flagellar motor (BFM) is the membrane-embedded rotary molecular motor which turns the flagellum that provides thrust to many bacterial species. [17] Behavior of the bacterial flagellar motor depends sensitively on the external loads it drives. [18] Reversible switching of the bacterial flagellar motor between clockwise (CW) and counterclockwise (CCW) rotation is necessary for chemotaxis, which enables cells to swim towards favorable chemical habitats. [19] ABSTRACT The bacterial flagellar motor (BFM) is a protein complex that confers motility to cells and contributes to survival and virulence. [20] The bacterial flagellar motor (BFM) is a rotary molecular motor embedded in the cell membrane of numerous bacteria. [21] In the bacterial flagellar motor, the cell-wall-anchored stator uses an electrochemical gradient across the cytoplasmic membrane to generate a turning force that is applied to the rotor connected to the flagellar filament. [22] Three classes of ion-driven protein motors have been identified to date: ATP synthase, the bacterial flagellar motor, and a proton-driven motor that powers gliding motility and the Type 9 protein secretion system (T9SS) in Bacteroidetes bacteria. [23] The bacterial flagellar motor is a bidirectional rotary motor for motility and chemotaxis, which often plays an important role in infection. [24] The bacterial flagellar motor is a unique supramolecular complex which converts ion flow into rotational force. [25] The bacterial flagellar motor is composed of a rotor and a dozen stators and converts the ion flux through the stator into torque. [26] The bacterial flagellar motor powers the rotation that propels the swimming bacteria. [27] The bacterial flagellar motor is an amazing nanomachine. [28] Here, we deployed cryo-electron tomography and genetic analysis to characterize in situ structure of the bacterial flagellar motor in Vibrio alginolyticus, which is best known for its polar sheathed flagellum and high-speed rotation. [29] The bacterial flagellar motor, a cell-envelope-embedded macromolecular machine that functions as a cellular propeller, exhibits significant structural variability between species. [30] The bacterial flagellar motor is a molecular machine that rotates the flagellar filament at high speed. [31] The bacterial flagellar motor, a large membrane-spanning ion-driven rotary motor that propels the bacteria to swim, provides a canonical example. [32] We combine the analogy with the use of bacterial flagellar motor as a single-cell "voltmeter" to measure cellular PMF in varied and dynamic external environments (for example, under different stresses). [33] The bacterial flagellar motor (BFM) powers the rotation that propels swimming bacteria. [34] The self‐assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio‐temporal synchronization of gene expression with proper protein localization and association of dozens of protein components. [35] The bacterial flagellar motor is an ion-powered transmembrane protein complex which drives swimming in many bacterial species. [36] The bacterial flagellar motor is a molecular machine that can rotate the flagellar filament at high speed. [37] The self-assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio-temporal synchronization of gene expression with proper protein localization and association of dozens of protein components. [38] The bacterial flagellar motor is driven by an ion flux that is converted to torque by motor-attendant complexes known as stators. [39] The bacterial flagellar motor accommodates ten stator units around the rotor to produce large torque at high load. [40] The bacterial flagellar motor is a rotary nanomachine driven by ion flow. [41] The bacterial flagellar motor is one of the most complex and sophisticated nanomachineries in nature. [42] We measure how the assembly of the bacterial flagellar motor depends on its operational parameters, such as speed and torque. [43]

Bidirectional Flagellar Motor

The bidirectional flagellar motor of the bacterium Escherichia coli recruits or releases torque-generating units (stator units) in response to changes in load. [1] Motility in many bacteria is powered by a bidirectional flagellar motor. [2]

flagellar motor protein

Sequencing and gene annotation results evidently showed presence of chemotaxis genes and flagellar motor proteins in Bacillus subtilis draft genome. [1] In the chemotaxis of Escherichia coli, the cell’s behavioral switch involves binding of the phosphorylated form of the chemotaxis signaling protein CheY (CheYp) to the flagellar motor protein FliM, which induces the motor to rotate clockwise; otherwise, the motor rotates counterclockwise. [2] The final speaker in the session was Sophie Hertel from the EMBL node for SingleMolecule Sciences at the University of New South Wales, who presented her recent attempts to assembly the flagellar motor protein Flig on immobilized designer DNA sequences in order to measure the kinetics of Flig protein interactions during motor assembly. [3] The reduction of swimming by ethanol required the flagellar motor proteins MotAB and two PilZ-domain proteins (FlgZ and PilZ). [4] This indicated that removal of the flagellar motor proteins, motAB (to reduce metabolic burden) and protein degradation machinery, clpX (to boost FT3SS levels intracellularly), result in high capacity secretion. [5] Six selective genes (lipoprotein-lipo, methyltransferase-MT, S-layer homology domain protein-BC, flagellar motor protein-motB, transcriptional regulator-XRE, crystal protein-cry2) and associated four novel plasmids were investigated along with the characteristics and expression profiles of two housekeeping genes (chaperonin protein-GroEL and topoisomerase enzyme-gyrB). [6]

flagellar motor switch

RT-PCR showed differential expression of treS (trehalose synthase), rpoS (sigma factor), mucA (alginate regulatory gene), and fliM (flagellar motor switch protein gene) in response to exposure to RH10%. [1] In addition, flagellar motor switch FliG gene silencing resulted in reduced bacterial motility. [2] The ligand and its complexes were subjected to in silico analysis against bacterial and fungal proteins such as flagellar motor switch G and MFS multidrug transporter (MFSmt), respectively using homology modelling tools to predict the structure of the proteins and molecular docking tools to analyze the activity of the synthesized compounds against the proteins. [3]

flagellar motor torque

A supercritical Hopf bifurcation in the flagellar orientation beyond a critical ratio of flagellar motor torque to hook bending stiffness, which is set by the spontaneous curvature of the flexible hook, the shape of the cell body, and the flagellum geometry, can have a dramatic effect on the cell’s trajectory through the fluid. [1] cholerae flagellar motor torque, and consequently, mucus penetration. [2]

flagellar motor require

The self‐assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio‐temporal synchronization of gene expression with proper protein localization and association of dozens of protein components. [1] The self-assembly of cellular macromolecular machines such as the bacterial flagellar motor requires the spatio-temporal synchronization of gene expression with proper protein localization and association of dozens of protein components. [2]

flagellar motor depend

Behavior of the bacterial flagellar motor depends sensitively on the external loads it drives. [1] We measure how the assembly of the bacterial flagellar motor depends on its operational parameters, such as speed and torque. [2]

flagellar motor significantly

Disruption of the flagellar motor significantly decreases host mortality of V. [1] campbellii pathogenesis, and disruption of the flagellar motor significantly decreases host mortality. [2]