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ETH Researchers Visualize the Binding of Proteins to the Nuclear Surface

January 15, 2003

Not only the genetic information of individual cells, but also that of the entire organism is stored within the cell nucleus. Each cell of a multicellular organism, e.g. man, contains the identical DNA sequences. The communication between the cell nucleus and the remainder of the cell is thus decisive for the correct functioning of the cells and guarantees the survival of the organism. The nuclear pore complex represent the only pathway for macromolecular communication between the cell nucleus and the rest of the cell.

Structural Properties Correlate with Functional Properties




Researchers of the ETH Institutes for Solid State Physics and Biochemistry have conducted in depth investigations of the nuclear pore complex and have answered the question as to whether the structure is altered by the binding of molecules. These molecules are, on the one hand, the so-called transport receptors, which are already known to be responsible for transport within the cell nucleus, and, on the other, alcohols. It was already known from earlier biochemical studies that the transport capacity of the pore complex is altered through the binding of these molecules. The studies in fact now show that the structure of the pore complex itself also changes, i.e. changes in the transport capacity into and out of the nucleus correlate with changes in the structure of the nuclear pore complex.

A Bridge from Physics to Biology

For their studies, the researchers used the so-called scanning force microscopy. With this method, a fine tip scans the surface of the cell and in this way produces a profile. By combining all the profiles measured, a three-dimensional picture of the surface investigated is created. However, biological structures are very different from those that are usually studied in physics. At the Institute for Solid State Physics of ETH Zurich the method of scanning force microscopy has been optimised, in order to also depict soft biological surfaces with great accuracy. In this way the ETH physicists have found a means by which biological structures – in this case nuclear pore complexes – can be investigated in their practically natural state. To achieve this they have joined forces with researchers from the Institute of Biochemistry.

ETH Zuerich



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