An alternative ‘fuel’ for cord-like motors in cells — ScienceDaily

Cells have an interesting ability to organize their interiors by generating directional movements using tiny protein machines called molecular motors. Most of them operate using a common type of fuel, a form of chemical energy called ATP. He is a researcher at the Physics of Excellence of Life (PoL), the Biotechnology Center of TU Dresden (BIOTEC) in Dresden, Germany, and the National Research Center. Biological Sciences (NCBS) in Bangalore, India, has discovered a new molecular system that uses alternative chemical energies and employs new mechanisms to perform mechanical work. By repeatedly contracting and expanding, this molecular motor functions similarly to a classical Stirling engine and helps distribute cargo to membrane-bound organelles. This is the first motor to use his two components of his two proteins of different sizes, Rab5 and EEA1, and instead of ATP he is driven by GTP. This result is published in Nature Physics.

Motor proteins are remarkable molecular machines within cells that convert chemical energy stored in a molecule called ATP into mechanical work. The most prominent example is myosin, which helps muscles move. In contrast, GTPases, which are small proteins, are not considered molecular force generators. One example is her molecular motor composed of two proteins, EEA1 and Rab5. In 2016, an interdisciplinary team of cell biologists and biophysicists in the group of MPI-CBG Directors Marino Zerial and Stephan Grill and their colleagues, including PoL and BIOTEC research group leader Marcus Jahnel, identified the small GTPase protein Rab5. can cause cell contraction. EEA1. These thread-like tether proteins can recognize and bind Rab5 proteins present in the vesicle membrane. Binding of the much smaller Rab5 sends messages along the elongated structures of EEA1, thereby increasing EEA1 flexibility. Such flexibility changes generate forces that pull the vesicles toward the target membrane where docking and fusion occur. However, the team also hypothesized that EEA1 could switch between flexible and fixed states by simply interacting with Rab5 alone, similar to the movement of a mechanical motor.

This was the beginning of the current study, shaped by the two PhDs who are the lead authors of this study. Joan Antoni Soler of Marino Zerial’s research group at MPI-CBG and Anupam Singh of Shashi Thutupalli’s group, a biophysicist at the Simons Center for the Study of Living Machines, NCBS, Bangalore, explored the behavior of this motor. attempted to be observed ly.

Anupam Singh spent three months at MPI-CBG in 2019 with an design in mind to investigate EEA1 protein dynamics. The experiments required specific modifications to the protein that allowed us to measure flexibility based on conformational changes,” he says. Joan Antoni Soler’s expertise in protein biochemistry was ideal for this challenging task. “We were pleased to learn that our approach to characterizing the EEA1 protein could answer whether EEA1 and Rab5 form a two-component motor, as previously suspected, and the difficulty of getting the right molecule. realized that a solution could be provided by modifying the EEA1 protein in such a way that fluorophores can be attached to specific protein regions. It makes it easier to characterize the changes that may occur in ,” explains Joan Antoni.

Armed with the right protein molecules and the invaluable support of co-author Janelle Lauer, a senior postdoctoral researcher in Marino Zerial’s research group, Joanne and Anupam used advanced laser scanning microscopy provided by the Light Microscopy Facility. , we were able to fully characterize the dynamics of EEA1. With MPI-CBG and NCBS. Strikingly, they found that the EEA1 protein can undergo multiple rigid-to-flexible flexibility transition cycles driven solely by chemical energy released by interaction with the GTPase Rab5. These experiments showed that EEA1 and Rab5 form her GTP-driven bicomponent motor. To interpret the results, Marcus Jahnel, one of the corresponding authors of PoL and BIOTEC and the leader of the research group, developed a new physical model to explain the coupling of chemical and mechanical steps in the motor his cycle. Developed. Together with Stephan Grill and Shashi Thutupalli, the biophysicist was also able to calculate the thermodynamic efficiency of the new motor system, which is comparable to his conventional ATP-driven motor protein.

“Our results show that proteins EEA1 and Rab5 function together as a two-component molecular motor system that can convert chemical energy into mechanical work. As a result, they are active mechanics in membrane trafficking. The force-generating molecular motion mechanisms are conserved across other molecules and may be used in several other cellular compartments,” says Marino Zerial. Summarizing the research, Marcus Jahnel adds: It has been considered a type of fuel, GTP, and primarily a signaling molecule. Put it in the light. Stephan Grill is equally excited. “This is a new class of molecular motor. It doesn’t move like the kinesin motors that transport cargo along microtubules, but it stays in place and does work. It’s a bit like the tentacles of an octopus. increase.”

“The model we used was inspired by that of the classical Stirling engine cycle. A conventional Stirling engine produces mechanical work by expanding and compressing gases, but the Two-component motors use proteins as working substrates, and forces are generated by changes in protein flexibility.As a result, this type of mechanism opens up new possibilities for the development of synthetic protein engines,” says Shashi Thutupalli. adds.

Overall, the authors hope that this new interdisciplinary study will open new research avenues in both molecular and cellular biology and biophysics.

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