The ribosome researcher

March 01, 2016

Marina Rodnina, Director at the Max Planck Institute for Biophysical Chemistry in Göttingen, receives the Gottfried Wilhelm Leibniz Prize 2016. The German Research Foundation (DFG) honors the biochemist for her pioneering contribution to the understanding of the functioning of ribosomes. The most important German science award is endowed with 2.5 million Euros.

Marina Rodnina, Max Planck Institute for Biophysical Chemistry in Göttingen

I am very happy that our work received this high recognition. Luckily I have a wonderful team working with me. This prize will allow us to address even more challenging questions in the field," said Marina Rodnina following the DFG announcement. The Managing Director of the Max Planck Institute for Biophysical Chemistry, Herbert Jäckle, congratulated the award winner: “It is always something special for scientists when their achievements are acknowledged by others. With her research on ribosomes, she has gained ground-breaking insights into an essential process of life – how cells produce proteins. The DFG honors this important work with the Leibniz Prize. We are very happy with Marina Rodnina and are proud of our colleague’s great success.” Marina Rodnina is now one of the 13 Leibniz Prize winners who presently carry out research at the institute or have worked here in the past.

Marina Rodnina succeeded in elucidating central principles of how ribosomes function. Her insights helped to understand the high precision of protein production. As “molecular workers”, proteins are involved in virtually all cellular activities. The proteins’ building plans are written down as genetic information in the DNA of each cell. During protein production, this genetic information is translated into a chain of amino acids which then folds into the three-dimensional structure of a protein. This translation is performed by the ribosome. The complex molecular machine itself consists of more than 50 protein components and three to four ribonucleic acid molecules. With a diameter of 20 to 30 nanometers (millionth of a millimeter) it is tiny. To investigate how it works is therefore extremely laborious and time-consuming.

To this end, Marina Rodnina and her team use different biophysical methods such as fluorescence measurements and techniques that monitor the course of fast chemical reactions. Her Department of Physical Biochemistry sets global standards when it comes to applying and further developing these complex methods to investigate ribosomes.

The scientist wants to find out how “incidents” in the protein factories are avoided. “The protein assembly has to be extremely accurate and deliver proteins with precisely the right spatial structure. Only then can they fully function. We want to understand which processes in the ribosome control the quality and how mistakes are avoided. Even small mistakes can be fatal for the cell,” the biochemist explains. Important basic principles of quality control have already been identified by Rodnina. In this context, her research mainly focused on the assembly of proteins in bacteria. Among other things she found out how the ribosome uses a mechanism known as induced fit to identify which amino acid is the right one for each individual position in the protein.

Another central objective of Rodnina’s research is to learn more about the ribosome’s structural dynamics. “While producing proteins the ribosome is constantly moving. We want to visualize these dynamics to better understand the processes at the protein factory.” Furthermore, the Max Planck researcher investigates “deliberate” mistakes of the ribosome: Occasionally, the nano machine has to make an apparent mistake in order to integrate an unusual amino acid into the protein. The biochemist strives to identify the molecular mechanisms controlling these exceptions to the rule.

For the upcoming years the scientist and her team already have ambitious plans: “We want to apply our methods to examine the protein production of higher cells such as yeast – a much more complex system.” The basic processes are similar to those in bacteria, but there are important differences. This is taken advantage of when using certain antibiotics: They block the bacterial ribosome only while sparing the protein factories of human cells. Understanding the structure and function of the ribosome is therefore indispensable for the development of new antibiotics in the future. “The Leibniz Prize gives us the freedom to now push ahead in this direction even faster,” the researcher says.

Along with Marina Rodnina, two further Max Planck scientists were awarded with the Leibniz Prize: Emmanuelle Charpentier from the Max Planck Institute for Infection Biology in Berlin, and Benjamin List of the Max-Planck-Institut für Kohlenforschung in Mülheim an der Ruhr.

(fk/cr)

 

 

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