The latest discovery that scientists have come through is molecular motors. Inside these motors, a cell possesses a remarkable ability to organize the interiors using a minuscule protein machine. It generates direct motion, and these motors rely on a common form of chemical energy (ATP) for functioning.
Researchers who belong to MPI-CBG, Cluster of Excellence Physics of Life (PoL), the Biotechnology Center (BIOTEC) of TU Dresden, and NCBS India went to another level and came up with a novel molecular system. It utilizes an alternative energy source and comes with a new mechanism for executing mechanical tasks. Keep going with the blog, and you will get to know about this new discovery.
Stirling engine uses repeated contraction and expansion like a molecular motor that operates pretty much on a familiar principle. It assists in the distribution of cargo to membrane-bound organelles. The molecular motor uses two components, two differently-sized proteins, Rab5 and EEA1. This is all done by GTP. All of these findings were published in the Nature Physics journal.
Motor proteins are outstanding molecular machines that have cells in them and then that are
converted into the chemical energy stored in a molecule known as ATP. One of the most prominent examples is myosin. It helps the muscles to move. In comparison, GTPases that are small proteins aren’t viewed as molecular force generators. For instance, the molecular motor which has composed of two proteins, EEA1 and Rab5.
What Experts Say About This
Back in 2016, there was an interdisciplinary team of cell biologists and biophysicists belonging to the MPI-CBG. Marino Zerial and Stephan Grill, along with their colleagues, including the PoL and BIOTEC research group and its leader Marcus Jahnel have discovered that the small GTPase protein Rab5 might trigger a contraction in EEA1. These proteins aid in recognizing the Rab5 protein, which is present in a vesicle membrane, and start binding to it.
The binding with the tiny Rab5 sends a message with an elongated structure of EEA1, which increases the flexibility, which is pretty much similar to how cooking can soften the spaghetti. The change seen in the flexibility will produce a force that should be able to pull a vesicle toward the target membrane, where docking and fusion occur. The team has also hypothesized that EEA1 can switch between flexible and rigid states. This is similar to a mechanical motor motion by simply interacting with the Rab5 alone.
What Latest Research Suggests
The current research which was done has said that, taking shape through the doctoral work of the two first authors of this study. Joan Antoni Soler, who’s export and is connected to Marino Zerial’s research group at MPI-CBG, and Anupam Singh, who is connected to the Shashi Thutupalli group, a biophysicist that works at the Simons Centre for the Study of Living Machines at the NCBS in Bangalore, India. Both of the experts have set out an experimental observation for this motor in action.
Coming up with an experimental design for investigating the dynamics of the EEA1 protein in mind. Anupam Singh was there for three months at the MPI-CBG back in 2019. He stated, ‘When I got to meet Joan, I told him about the idea of computing and calculating the protein dynamics of EEA1. All of these experiments want specific modifications done to the protein, allowing for measuring the flexibility based on its structural changes.’
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Meanwhile, Joan Antoni Soler, who’s an expert in protein biochemistry who’s a perfect fit for this challenging task, has stated, ‘I was delighted to learn about the approach for characterizing the EEA1 protein that can answer whether EEA1 and Rab5 forms a two-component motor as it was previously suspected. Then I realized all of the difficulties that we have faced while obtaining correct molecules might be solved by modifying the EEA1 protein, as it will allow fluorophores to attach to specific protein regions.
The suitable protein molecules and the valuable support of the co-author, Janelle Lauer, a senior postdoctoral researcher in the research group where Joan and Anupam did the characterization of the dynamics of EEA1. They did all of this by utilizing the advanced laser scanning microscopes which were provided by MPI-CBG and the NCBS.
The discovery of EEA1 protein can undergo multiple flexibility transition cycles, from rigid to flexible and back again. All of this can be driven solely by the chemical energy which was released by its interaction with the GTPase Rab5. These experiments, which were done, have shown that EEA1 and Rab5 form a GTP-driven two-component motor.
For interpreting the results, Marcus Jahnel, a corresponding author and a research group leader at PoL and BIOTEC, has come up with a physical model that explains the coupling between chemical and mechanical steps in the motor.
Marino Zerial has summarized the study and said, ‘Our results show that the proteins EEA1 and Rab5 work together flawlessly as a two-component molecular motor system which will be able for transferring chemical energy into the mechanical work, which results in let them play active mechanical roles in membrane trafficking. All this makes it possible for the force-generating molecular motor mechanism to be conserved across other molecules, which was used by several other cellular compartments.’
While Marcus Jahnel has added, ‘We are happy that we can finally test the idea of an EEA1-Rab5 motor. It is so good to see that it is confirmed by these new experiments. Many molecular motors use a very common option of cellular fuel, which is called ATP. Many GTPases consume different types of fuel GTP and have been used as signaling molecules. It can also drive a molecular system for creating or generating forces and put these abundant molecules in an interesting new light.’
With all the discoveries that are happening in this world, the Molecular Motor is one of those discoveries that will be coming in handy for many researchers and scientists out there in this world. It will help them in bringing out the best results for their tests and sampling.
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