1

Tanyut Huidrom

Professor Sougata Roy

Physiology BIO-3423/ BIO-6423-1

5 March 2023

Assignment 3: Chemotaxis

Chemotaxis is the process by which cells move towards or away from a chemical gradient.

The cells detect changes in the concentration of chemical molecules in their environment and

respond by moving towards or away from the source of the chemical signal.

In Escherichia coli, chemotaxis is mediated by a complex signaling pathway that involves

the binding of environmental stimuli to chemoreceptors on the cell surface. The chemoreceptors

are connected to a cytoplasmic signaling complex that regulates the activity of the flagellar

motor, which propels the bacteria through liquid environments. When a chemoreceptor is

activated, it stimulates the cytoplasmic signaling complex to induce changes in the direction of

flagellar rotation, causing the bacteria to move towards or away from the source of the chemical

signal.

Flagellar motor: The flagellar motor is a complex molecular machine composed of a series of

proteins that work together to rotate the flagellum. The motor is anchored to the cell wall and

consists of a rotor, stator, and filament. The rotor is composed of a protein called FliG, which
 2

interacts with another protein complex in the stator. The stator is made up of two proteins, MotA

and MotB, which form a channel through which ions can pass. The flow of ions through the

channel generates a proton motive force that drives the rotation of the rotor and flagellum.

Chemotaxis signaling pathway: The chemotaxis signaling pathway allows E. coli to sense and

respond to changes in its environment. The pathway is composed of a series of proteins that

interact with each other to transmit signals from the environment to the flagellar motor. The

pathway begins with the binding of environmental stimuli to chemoreceptors on the cell surface.

The chemoreceptors are connected to a cytoplasmic signaling complex, which consists of the

protein CheA, the adaptor protein CheW, and the response regulator protein CheY. When a

chemoreceptor is activated, it stimulates the cytoplasmic signaling complex to phosphorylate

CheY. The phosphorylated form of CheY binds to the flagellar motor and induces a change in the

direction of flagellar rotation. This change in direction causes the cell to move towards or away

from the source of the environmental stimulus.

Cytoplasmic signaling complex: The cytoplasmic signaling complex is a protein complex that

regulates the activity of the flagellar motor in response to signals from the environment. The

complex consists of three proteins: CheA, CheW, and CheY. CheA is a protein kinase that

phosphorylates CheY in response to signals from the chemoreceptors. CheW is an adaptor

protein that connects CheA to the chemoreceptors, allowing the complex to respond to changes

in the environment. CheY is a response regulator protein that binds to the flagellar motor and

regulates its activity.

 3

The direction of flagellar rotation in E. coli plays a crucial role in determining the direction of

bacterial movement. When the flagellar motor rotates counterclockwise, the flagella bundle

together to propel the cell forward in a straight line, which is known as a "run." However, when

the flagellar motor rotates clockwise, the flagella comes apart and the cell tumbles, changing its

direction of movement. The ability of E. coli to switch between running and tumbling is

important for its ability to navigate its environment during chemotaxis. When E. coli encounters

a chemical attractant, the binding of the attractant to its chemoreceptors causes the flagellar

motor to rotate counterclockwise, resulting in a net movement towards the attractant. However,

when the concentration of the attractant decreases or the bacterium encounters a repellent, the

chemoreceptors signal the flagellar motor to switch to clockwise rotation, causing the bacterium

to tumble and change its direction of movement.

4
 5

Works Cited

Hansen, Clinton H et al. “Chemotaxis in Escherichia coli: a molecular model for robust precise

adaptation.” PLoS computational biology vol. 4,1 (2008): e1.

doi:10.1371/journal.pcbi.0040001