In this chapter, we have examined coupled transport systems that rely on ATP hydrolysis, on primary gradients of \(\mathrm{Na}^{+}\) or \(\mathrm{H}^{+},\) and on phosphotransferase systems. Suppose you have just discovered an unusual strain of bacteria that transports rhamnose across its plasma membrane. Suggest experiments that would test whether it was linked to any of these other transport systems.

Short Answer

Expert verified
To test for linkage to ATP hydrolysis, introduce ATP hydrolysis inhibitors and observe if rhamnose uptake decreases. For a link to \(\mathrm{Na}^{+}\) or \(\mathrm{H}^{+}\) gradients, introduce a gradient destruction agent and see if rhamnose uptake decreases. And to test for a link to phosphotransferase systems, introduce specific inhibitors of phosphotransferase systems and check for decrease in rhamnose uptake.

Step by step solution

01

Linkage to ATP Hydrolysis

An experiment can be designed by using metabolic inhibitors of ATP hydrolysis. Place the bacteria in a medium with rhamnose and observe its rate of uptake. Then introduce the ATP hydrolysis inhibitors and monitor the rate again. If the transportation of rhamnose is linked to ATP hydrolysis, a significant decrease in the rate will be seen.
02

Linkage to Sodium or Proton Gradients

One can use a proton or sodium ion gradient destruction agent in the next experiment. The bacteria is first placed in a rhamnose-rich medium and the rhamnose uptake is monitored. When a gradient-destruction agent (a substance that equalizes proton or sodium concentration) is introduced, a decrease in rhamnose uptake would signify a link to either proton or sodium gradients.
03

Linkage to Phosphotransferase Systems

Introducing a specific inhibitor of phosphotransferase systems would be the strategy here. The initial uptake of rhamnose is observed, then the inhibitor is added. If the rhamnose uptake decreases significantly after the introduction of the inhibitor, this would imply that the bacterium's transport of rhamnose is linked to phosphotransferase systems.

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Key Concepts

These are the key concepts you need to understand to accurately answer the question.

ATP Hydrolysis
One of the primary ways cells store and use energy is through a process known as ATP hydrolysis. ATP, or adenosine triphosphate, is often referred to as the energy currency of the cell. The molecule consists of a ribose sugar, an adenine base, and three phosphate groups. The bonds between these phosphate groups contain potential energy that, when broken via hydrolysis (reaction with water), release energy that the cell can harness for various activities including active transport mechanisms.

When cells need to power transportation of substances across membranes, such as with rhamnose in bacteria, they often rely on the energy from ATP hydrolysis. By linking the transport of rhamnose to ATP hydrolysis, bacteria can effectively move this sugar against its concentration gradient into the cell, which is essential for its metabolism and function.

As outlined in the textbook steps, observing a decrease in rhamnose uptake in the presence of metabolic inhibitors of ATP hydrolysis would affirm the role of ATP in the transport process. Such experiments highlight the critical nature of ATP in providing the necessary energy to drive many cellular transport systems.
Ion Gradient Coupled Transport
Another fascinating transport mechanism is the ion gradient coupled transport, which uses the energy stored in the form of ion concentration differences across the cell membrane. Cells maintain gradients of ions like sodium (a+)) and protons (H+)), which possess potential energy due to the concentration differences between the inside and outside of the cell.

This gradient represents a form of stored energy that can be used to drive the transport of other substances. In the context of bacterial rhamnose transportation, if the uptake of rhamnose is coupled to the dissipation of these ion gradients, it would mean the transport process is energetically coupled to the movement of ions.

As suggested in the textbook solution, introducing an agent that dissipates the ion gradient and leads to a reduced rhamnose uptake would support the hypothesis that rhamnose transport is linked to ion gradients. This is a crucial concept in understanding not only how substances are transported into and out of cells but also how cells utilize and manage energy.
Phosphotransferase Systems
Phosphotransferase systems (PTS) present yet another ingenious manner in which bacteria can transport sugars like rhamnose. This system involves a series of proteins that transfer a phosphate group from phosphoenolpyruvate (PEP) to the sugar as it is transported into the cell. By phosphorylating the sugar, the PTS provides a dual advantage: actively transporting the sugar while simultaneously preparing it for metabolism.

The importance of this system in bacterial transport can be addressed experimentally, as proposed in the textbook exercise. By adding an inhibitor specific to the PTS and observing a consequent decrease in rhamnose uptake, one can provide strong evidence that rhamnose transport in the bacterial strain is dependent on a phosphotransferase system. This kind of transport is particularly noteworthy because it ties the transport process directly to the metabolic pathway of the sugar, reflecting the efficiency of bacterial systems in coupling transport and metabolism.

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Most popular questions from this chapter

In the description of the mechanism of proton transport by bacteriorhodopsin, we find that light-driven conformation changes promote transmembrane proton transport. Suggest at least one reason for this behavior. In molecular terms, how could a conformation change facilitate proton transport?

The purple patches of the Halobacterium halobium membrane, which contain the protein bacteriorhodopsin, are approximately \(75 \%\) protein and \(25 \%\) lipid. If the protein molecular weight is 26,000 and an average phospholipid has a molecular weight of 800 , calculate the phospholipid-to-protein mole ratio.

As described in the text, the \(\mathrm{pK}_{\mathrm{a}}\) values of Asp \(^{85}\) and \(\mathrm{Asp}^{96}\) of bacteriorhodopsin are shifted to high values (more than 11 ) because of the hydrophobic environment surrounding these residues. Why is this so? What would you expect the dissociation behavior of aspartate carboxyl groups to be in a hydrophobic environment?

Proline residues are almost never found in short \(\alpha\) -helices; nearly all transmembrane \(\alpha\) -helices that contain proline are long ones (about \(20 \text { residues }) .\) Suggest a reason for this observation.

As described in this chapter, proline introduces kinks in transmembrane \(\alpha\) -helices. What are the molecular details of the kink, and why does it form? A good reference for this question is von Heijne, G. 1991\. Proline kinks in transmembrane \(\alpha\) -helices. Journal of Molecular Biology \(218: 499-503 .\) Another is Barlow, D. \(\mathrm{J}\)., and Thornton, J. M., \(1988 .\) Helix geometry in proteins. Journal of Molecular Biology \(201: 601-619\)

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