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Single-molecule technique captures calcium sensor calmodulin in action
Date:8/14/2009

It's well known that the protein calmodulin specifically targets and steers the activities of hundreds of other proteins mostly kinases in our cells, thus playing a role in physiologically important processes ranging from gene transcription to nerve growth and muscle contraction But just how it distinguishes between target proteins is not well understood. Methods developed by biophysicists at the Technische Universitaet Muenchen (TUM) have enabled them to manipulate and observe calmodulin in action, on the single-molecule scale. In recent experiments, as they report in the early edition of PNAS, the Proceedings of the National Academy of Sciences, they compared the sequences of structural and kinetic changes involved in binding two different kinases. The results reveal new details of how calmodulin binds and regulates its target proteins.

A so-called signaling protein and "calcium sensor," calmodulin gives start and stop signals for a great number of intracellular activities by binding and releasing other proteins. Calmodulin can bind up to four calcium ions, and the three-dimensional spatial structure of calmodulin varies with the number of calcium ions bound to it. This structure in turn helps to determine which amino acid chains peptides and proteins the calmodulin will bind.

Techniques such as X-ray structural analysis offer snapshots, at best, of steps in this intracellular work flow. But single-molecule atomic-force spectroscopy has opened a new window on such dynamic processes.

Professor Matthias Rief and colleagues at the Technische Universitaet Muenchen had previously shown that they could fix a single calmodulin molecule between a surface and the cantilever tip of a specially built atomic-force microscope, expose it to calcium ions in solution, induce peptide binding and unbinding, and measure changes in the molecule's mechanical properties as it did its work.

"What is special about our technique," R
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Contact: Patrick Regan
regan@zv.tum.de
49-892-892-2743
Technische Universitaet Muenchen
Source:Eurekalert  

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