Discovery of how a key enzyme of the spliceosome exerts its controlling function

Structure of Brr2-protein belongs to a family of enzymes that are called “RNA helicases”.

Structure of Brr2-protein belongs to a family of enzymes that are called “RNA helicases”.

To sustain life, processes in biological cells have to be strictly controlled both in time and in space. By using the MX-Beamline of synchrotron radiation source BESSY II research workers at the Max Planck Institute for Biophysical Chemistry in Göttingen and the Free University of Berlin have elucidated a previously unknown mechanism that regulates one of the essential processes accompanying gene expression in higher organisms. In humans, errors in this control mechanism can lead to blindness. This discovery has been published in the renowned scientific journal Science (23th may 2013).

Traudy Wandersleben and Karine Santos from the research group of Markus Wahl in Berlin determined the atomic structure of the Brr2 protein in contact with the relevant regulatory portion of Prp8. “To do this we used X ray crystallography,” states Markus Wahl. “There are excellent facilities for this kind of research at the BESSY II synchrotrons at the Helmholtz Centre in Berlin, where the necessary specialised instrumentation is available”.

Please find here the complete press release published by Freie Universität Berlin.

Original paper

Mozaffari Jovin, S., Wandersleben, T., Santos, K.F., Will, C.L., Lührmann, R., Wahl, M.C. (2013) Inhibition of RNA helicase Brr2 by the C-terminal tail of the spliceosomal protein Prp8. Science, 23 Mai 2013. DOI: ...

Further publications on the subject

[1]    Santos, K. F., Mozaffari Jovin, S., Weber, G., Pena, V., Lührmann, R., Wahl, M. C. (2012) Structural basis for functional cooperation between tandem helicase cassettes in Brr2-mediated remodeling of the spliceosome. Proc. Natl. Acad. Sci. USA 109, 17418-17423.

[2]    Mozaffari Jovin, S., Santos, K. F., Hsiao, H.-H., Will, C. L., Urlaub, H., Wahl, M. C., Lührmann, R. (2012) The Prp8 RNase H-like domain inhibits Brr2-mediated U4/U6 snRNA unwinding by blocking Brr2 loading onto the U4 snRNA. Genes Dev. 26, 2422-2434.

Further information::
Homepage of MPI-group Göttingen

Homepage of FU-group Berlin


übernommen von FU

You might also be interested in

  • HZB receives funding to make innovations usable more quickly
    News
    23.03.2023
    HZB receives funding to make innovations usable more quickly
    The Helmholtz Association has selected three new innovation platforms that will now be funded. HZB is involved in two of them: The Innovation Platform on Accelerator Technologies HI-ACTS is intended to open up modern accelerators for a wide range of applications, while the Innovation Platform Solar TAP is intended to bring new ideas from the laboratories of photovoltaics research more quickly into an application. In total, HZB will receive 4.2 million euros in grants from the Pact for Research and Innovation over the next three years.


  • Perovskite solar cells from the slot die coater - a step towards industrial production
    Science Highlight
    16.03.2023
    Perovskite solar cells from the slot die coater - a step towards industrial production
    Solar cells made from metal halide perovskites achieve high efficiencies and their production from liquid inks requires only a small amount of energy. A team led by Prof. Dr. Eva Unger at Helmholtz-Zentrum Berlin is investigating the production process. At the X-ray source BESSY II, the group has analyzed the optimal composition of precursor inks for the production of high-quality FAPbI3 perovskite thin films by slot-die coating. The solar cells produced with these inks were tested under real life conditions in the field for a year and scaled up to mini-module size.
  • Superstore MXene: New proton hydration structure determined
    Science Highlight
    13.03.2023
    Superstore MXene: New proton hydration structure determined
    MXenes are able to store large amounts of electrical energy like batteries and to charge and discharge rather quickly like a supercapacitor. They combine both talents and thus are a very interesting class of materials for energy storage. The material is structured like a kind of puff pastry, with the MXene layers separated by thin water films. A team at HZB has now investigated how protons migrate in the water films confined between the layers of the material and enable charge transport. Their results have been published in the renowned journal Nature Communications and may accelerate the optimisation of these kinds of energy storage materials.