Phosphate Balance In Higher Organisms Elucidated

Chemists and biochemists at the Ruhr University, working in collaboration with research scientists at the European Molecular Biology Laboratory in Heidelberg and the University of Lausanne, have now gained insight into the basic data on the formation mechanism of polyphosphate chains.

The scientists have been able to identify the first x-ray structure of the enzyme responsible for the biosynthesis of polyphosphates in highly developed organisms (eukaryotes) and to distinguish the basic biochemical processes. The molecular catalytic processes can be accurately described based on the data obtained. This knowledge constitutes the foundation for further targeted research into the role of polyphosphates. The scientists have published their results in the current edition of the journal Science.

The enzyme investigated - VTC (vacuolar transporter chaperone) - makes use of the universal “energy carrier” ATP (adenosine triphosphate) within cells for the gradual synthesis of phosphate chains. A depot, which the organism can resort to under stress conditions, is thus created. Using structure-biological and biophysical methods, the scientists were able to show which molecular tools the enzyme uses for the reorganization of the phosphates from the source into the depot.

Prof. Christian Herrmann (Physical Chemistry I) explained that the structure of the chain-shaped depot substance and its simultaneous transport in a cellular subunit with the aid of a tunnel-shaped protein structure is of particular interest. The VTC enzyme is part of a large protein complex that reaches the cell via an inner membrane. Its characterization is a milestone for research into ATP-dependent membrane processes.