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Proteins shine a brighter light on cellular processes
Date:3/20/2012

ant X-ray beams at the ESRF, the teams from Grenoble and Oxford uncovered subtle details of how CFPs store incoming energy and retransmit it as fluorescent light: they produced tiny crystals of many different improved CFPs and resolved their molecular structures. These structures revealed a subtle process near the so-called chromophore, the light-emitting complex inside the CFPs, whose fluorescence efficiency could be modulated by the environment. "We could understand the function of individual atoms within CFPs and pinpoint the part of the molecule that needed to be modified to increase the fluorescence yield" says David von Stetten from the ESRF.

In parallel to this work, the Amsterdam team led by Theodorus Gadella used an innovative screening technique to study hundreds of modified CFP molecules, measuring their fluorescence lifetimes under the microscope to identify which had improved properties.

The result of this rational design is a new CFP, called mTurquoise2. By combining structural and cellular biology efforts, the researchers managed to show that mTurquoise2 has a fluorescence efficiency of 93%, unmatched for this type of proteins.

The new molecule will allow life scientists to study protein-protein interactions in living cells with unprecedented sensitivity. High sensitivity matters in processes where only a few proteins are involved and signals are weak, and in fast reactions where the time available for accumulating fluorescent light is short.

"With the new protein, many studies can now be performed with levels of accuracy and detail that were impossible yesterday. Moreover, thanks to this novel approach taking into account the structural dynamics of the protein, scientists now hope to design improved fluorescent proteins emitting light of different colours for use in other applications" concludes Antoine Royant.


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Contact: Claus Habfast
claus.habfast@esrf.fr
33-476-882-128
European Synchrotron Radiation Facility
Source:Eurekalert  

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