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Intracellular express -- why transport protein molecules have brakes
Date:5/21/2010

enabled the scientists to measure the force with which the motor protein can pull. In this experimental setup, the kinesin-2 with its freight walks as far as 1,500 nanometers in tiny steps measuring a mere eight nanometers. "If we didn't hold it back, it might still go a lot further," says Zeynep kten from the Institute for Cell Biology at LMU.

The kinesin-2 investigated consists of one KLP11 and one KLP20 protein. By exchanging the heads of the chains, the researchers were able to show that KLP11 is a non-processive motor protein. It only becomes a transport protein in combination with KLP20. In further experiments they were able to explain why nature chooses this unusual combination: KLP20 proteins have no "brakes." A transport protein made of two KLP20 units would be permanently on the go and would waste energy. The KLP11, in contrast, has a mechanism called autoinhibition, which makes sure that the transport protein is at a standstill if no freight is attached.

"Our results show that a molecular motor must take on a large number of functions over and above simple transport, if it wants to operate successfully in a cell," says Professor Matthias Rief from the Physics Department of the TU Muenchen. It must be possible to switch the motor on and off, and it must be able to accept a load needed at a specific location and hand it over at the destination. "It is impressive how nature manages to combine all of these functions in one molecule," Rief says. "In this respect it is still far superior to all the efforts of modern nanotechnology and serves as a great example to us all."


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Contact: Patrick Regan
regan@zv.tum.de
49-892-891-0515
Technische Universitaet Muenchen
Source:Eurekalert

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