Difference between revisions of "Team:Technion Israel/Chemotaxis"

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Bacteria are able to sense a vast range of environmental signals, from nutrient and toxin concentrations
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Chemotaxis enables bacteria to The ability to sense their immediate environment and quickly adapt to changes in it.  
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to oxygen levels. In such a dynamic setting, the ability to  
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The ability to sense changes in the environment and quickly respond to them is essential to the cell's life <b>(3)</b>.  
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sense changes in the environment and quickly respond to them is essential to the cell's life <b>(3)</b>.  
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The bacterial chemotaxis system has evolved to answer this need.<br>
 
The bacterial chemotaxis system has evolved to answer this need.<br>
 
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Chemotaxis is the movement of an organism towards or away from a chemical stimulus.  
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Chemotaxis is the movement of an organism towards or away from a chemical stimulus, as is presented in figure 1.  
 
The most common sensory pathways in prokaryotes use a chemotaxis system that contains  
 
The most common sensory pathways in prokaryotes use a chemotaxis system that contains  
 
at least two components - a dimeric histidine protein kinase (HPK) and a response regulator (RR).<br>
 
at least two components - a dimeric histidine protein kinase (HPK) and a response regulator (RR).<br>
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Chemo-sensing is carried out by a broad repertoire of chemoreceptors. Most have a N-terminal
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<br>(Add an image of tal – bacteria sense chemotaxis)</b>
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region that spans the membrane twice, which results in an intertwined periplasmic domain that
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<b>Fig. 1:</b> Chemotaxis concept. Adapted from <a href="https://2012.igem.org/Team:Goettingen/Project" ><b>iGEM gottingen 2012</b></a> <br>
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can sense an extracellular signal. The C-terminal cytoplasmic region comprises a
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<a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true"
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data-content="an approximately 50 amino acid region that connects the extracellular sensory
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domain with the intracellular signaling domain in over 7500 proteins, including histidine
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kinases, adenylyl cyclase, chemotaxis receptors, and phosphatases domain.">
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HAMP<i class="entypo-check"></i></button></a>, a dimerization domain and a kinase domain
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that interacts with its RR <b>(3)</b><br>
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Ligands bind to the periplasmic domain of the chemoreceptor at the interface between the
 
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two monomers of the dimer, with residues from both monomers being involved in the binding
 
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process. Ligand binding alters the interactions between the periplasmic domains, and
 
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between the transmembrane dimer <b>(3)</b>.<br>
 
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The activation of the receptor by an external stimulus causes auto-phosphorylation in the <a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true" data-content="Multifunctional proteins, of the transferase class of enzymes, that play a role in signal transduction across the cellular membrane."> histidine kinase</a>,
 
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CheA. CheA, in turn, transfers phosphoryl groups to residues in the
 
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response regulators CheB and CheY. This mechanism of signal transduction is called <a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true" data-content="Serves as a basic stimulus-response coupling mechanism to allow organisms to sense and respond to changes in many different environmental conditions."> two component system</a>, and is common form of signal transduction in bacteria <b>(1)</b>.
 
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<p class="text-center"><b>Fig. 1:</b> Signaling components and circuit logic <b>(2)</b>.</p>
 
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<br>
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Chemo-sensing is carried out by a broad repertoire of chemoreceptors. Most have a N-terminal
 +
region that spans the membrane twice, which results in an intertwined periplasmic domain that
 +
can sense an extracellular signal. The C-terminal cytoplasmic region comprises a
 +
<a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true"
 +
data-content="an approximately 50 amino acid region that connects the extracellular sensory
 +
domain with the intracellular signaling domain in over 7500 proteins, including histidine
 +
kinases, adenylyl cyclase, chemotaxis receptors, and phosphatases domain.">
 +
HAMP<i class="entypo-check"></i></button></a>, a dimerization domain and a kinase domain
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that interacts with its RR <b>(3)</b><br>
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</p>
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<p class="text-justify">
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Ligands bind to the periplasmic domain of the chemoreceptor at the interface between the
 +
two monomers of the dimer, with residues from both monomers being involved in the binding
 +
process. Ligand binding alters the interactions between the periplasmic domains, and
 +
between the transmembrane dimer <b>(3)</b>.<br>
 +
<br>
 +
The activation of the receptor by an external stimulus causes auto-phosphorylation in the <a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true" data-content="Multifunctional proteins, of the transferase class of enzymes, that play a role in signal transduction across the cellular membrane."> histidine kinase</a>,
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CheA. CheA, in turn, transfers phosphoryl groups to residues in the
 +
response regulators CheB and CheY. This mechanism of signal transduction is called <a data-toggle="popover" data-trigger="click" data-original-title="Info:" data-html="true" data-content="Serves as a basic stimulus-response coupling mechanism to allow organisms to sense and respond to changes in many different environmental conditions."> two component system</a>, and is common form of signal transduction in bacteria <b>(1)</b>.
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<a class="pop ocenter">
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<img src="https://static.igem.org/mediawiki/2016/6/6c/T--Technion_Israel--Chemotaxis1.PNG" class="img-responsive img-center" width="450" style="cursor: pointer;">
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</a>
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<p class="text-center"><b>Fig. 1:</b> Signaling components and circuit logic <b>(2)</b>.</p>
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Revision as of 13:23, 18 October 2016

S.tar, by iGEM Technion 2016

S.tar, by iGEM Technion 2016

Chemotaxis explained

Chemotaxis enables bacteria to The ability to sense their immediate environment and quickly adapt to changes in it. The ability to sense changes in the environment and quickly respond to them is essential to the cell's life (3). The bacterial chemotaxis system has evolved to answer this need.

Chemotaxis is the movement of an organism towards or away from a chemical stimulus, as is presented in figure 1. The most common sensory pathways in prokaryotes use a chemotaxis system that contains at least two components - a dimeric histidine protein kinase (HPK) and a response regulator (RR).


(Add an image of tal – bacteria sense chemotaxis) Fig. 1: Chemotaxis concept. Adapted from iGEM gottingen 2012

The E.coli chemotaxis system is considered a model system that demonstrates some of the core principles of chemotaxis. Through use of its flagella, E.coli has the ability to move rapidly towards attractants and away from repellents, by means of a random movement, with “runs” and “tumbles” by rotating its flagellum counter-clockwise and clockwise, respectively.

Fig. 2: Random and run movement of E.coli. (2).


When E.coli moves in a medium that lacks a concentration gradient – the cell travels, stops or tumbles and then continues moving in a new random direction.

When the flagella rotate counter-clockwise it forms a tight bundle and directs the cell forward in a straight running motion. After a brief period, the direction of rotation is reversed, causing a tumble. As the cell moves up the chemical gradient the runs become longer in comparison to moving down the gradient.

The overall result is random movement in the absence of a chemical gradient , and movement towards or away from a chemical when a gradient exists (3).


Chemo-sensing is carried out by a broad repertoire of chemoreceptors. Most have a N-terminal region that spans the membrane twice, which results in an intertwined periplasmic domain that can sense an extracellular signal. The C-terminal cytoplasmic region comprises a HAMP, a dimerization domain and a kinase domain that interacts with its RR (3)

Ligands bind to the periplasmic domain of the chemoreceptor at the interface between the two monomers of the dimer, with residues from both monomers being involved in the binding process. Ligand binding alters the interactions between the periplasmic domains, and between the transmembrane dimer (3).

The activation of the receptor by an external stimulus causes auto-phosphorylation in the histidine kinase, CheA. CheA, in turn, transfers phosphoryl groups to residues in the response regulators CheB and CheY. This mechanism of signal transduction is called two component system, and is common form of signal transduction in bacteria (1).

Fig. 1: Signaling components and circuit logic (2).

References:
1. GREBE, Thorsten W.; STOCK, Jeff. Bacterial chemotaxis: the five sensors of a bacterium. Current Biology, 1998, 8.5: R154-R157.

2. John S. Parkinson, An overview of E. coli chemotaxis, Biology Department, University of Utah

3. WADHAMS, George H.; ARMITAGE, Judith P. Making sense of it all: bacterial chemotaxis. Nature Reviews Molecular Cell Biology, 2004, 5.12: 1024-1037.‏

4. WANG, Qingfeng, et al. Sensing wetness: a new role for the bacterial flagellum. The EMBO journal, 2005, 24.11: 2034-2042.‏




S.tar, by iGEM Technion 2016