Göttinger Graduiertenschule für Neurowissenschaften, Biophysik und Molekulare Biowissenschaften

Rodnina, Marina, Prof. Dr.

Professor of Biochemistry

  • PhD, Institute of Molecular Biology and Genetics, Academy of Science Ukraine, Kiew, Ukraine, 1989
  • Research Fellow of the Alexander von Humboldt Foundation, University of Witten, Germany, 1990-1992
  • Research Fellow at the Institute of Molecular Biology, University of Witten/Herdecke, 1992-1998
  • Associate Professor for Physical Biochemistry at the Institute of Molecular Biology, University of Witten/Herdecke, 1998-2000
  • Full Professor, Head of the Institute of Physical Biochemistry, University of Witten/Herdecke, 2000-2008
  • Director of Department of Physical Biochemistry, Max Planck Institute for Biophysical Chemistry, Göttingen, since 2008

Major Research Interests

1. Ribosome function and dynamics
2. Regulation and fidelity of translation
3. Ribosome-catalyzed reactions

Protein synthesis from amino acids in the cell is performed on ribosomes, large ribonucleoprotein particles that consist of several RNA molecules and over 50 proteins. The ribosome is a molecular machine that selects its substrates, aminoacyl-tRNAs, very rapidly and accurately and catalyses the synthesis of peptides from amino acids. Among the most important unresolved questions is the role of structural dynamics in ribosome function. The communication between the functional centers of the ribosome is known to be crucial, but there are only vague ideas as to how this may take place. The activation of the GTPase of elongation factor (EF)-Tu is a key step in selection of aminoacyl tRNAs by the ribosome. It is triggered by events on the small subunit, but the GTP-binding site of EF-Tu associates with the large subunit, and the way the signal is transmitted within the ribosome remains unknown. The mechanism of the translocation step, i.e. the movement of tRNAs and mRNA through the ribosome, remains a major challenge. EF-G accelerates translocation by using the energy of GTP hydrolysis to drive translocation which resembles the way motor proteins work; however, the structural basis for the movement and its biophysical characteristics are not known. Finally, incorporation of unusual amino acids, such as selenocysteine, requires highly specialized machinery for delivery; very little is known about the molecular mechanism of this process. None of these problems can be solved without using a combination of techniques from Biochemistry, Structural Biology and Physical Biochemistry and developing new approaches to structure, function, and dynamics of the translational apparatus. In a broader context, the ribosome can serve as a well-characterized model of large macromolecular assemblies. Using the biophysical approaches devised for the ribosome, it should be possible to obtain information for even larger and more complex macromolecular assemblies. Developing of highly efficient and controlled ribosome translation systems on a highly sophisticated technological level is important for production of proteins with desired properties for purposes of proteomics and high-throughput structural studies emerging in the post-genomic era. The translational apparatus is a major target for antibiotics. Better understanding of the mechanisms of antibiotic action, resistance mechanisms and the interplay between resistance and bacterial fitness using systems biology will be increasingly important for developing new antimicrobials and combating the major infectious diseases

Homepage Department/Research Group


Selected Recent Publications

  • Caliskan N, Wohlgemuth I, Korni, N, Pearson M, Peske F, Rodnina MV (2017) Conditional switch between frameshifting regimes upon translation of dnaX mRNA. Mol Cell 66, 558-567.
  • Belardinelli R, Sharma H, Caliskan N, da Cunha CEL, Peske F, Wintermeyer W, Rodnina MV (2016) Choreography of molecular movements during ribosome progression along mRNA. Nat Struct Molec Biol 23:342-348.
  • Holtkamp W, Kokic G, Jäger M, Mittelstaet J, Komar AA, Rodnina MV (2015) Co-translational protein folding on the ribosome monitored in real time. Science 350:1104-1107.
  • Maracci C, Peske F, Dannies E, Pohl C, Rodnina MV (2014) Ribosome-induced tuning of GTP hydrolysis by a translational GTPase. Proc Natl Acad Sci USA 111:14418-14423.
  • Doerfel LK, Wohlgemuth I, Kothe C, Peske F, Urlaub H, Rodnina MV (2013) EF-P is essential for rapid synthesis of proteins containing consecutive proline residues. Science 339, 85-88.