Virtual Spring School CRC902

On Thursday, 27/28th April, 12 pm to 6 pm

In this meeting the students of the IRTG will present their projects, listen to invited speakers, discuss with the PIs from the SFB902 and enjoy a green lab workshop.

Our goals for this year’s Spring School are the following:

  • Get and provide feedback to the PhD and postdoc projects of all CRC902 projects
  • Learn about the Science of our ‘biological’, ‘chemical’ and ‘technological’ groups of the SFB902 
  • Vote for the Price of the best talk
  • Transmit the passion about different aspects of RNA research
  • Strengthen the bonds between all early career scientists of the CRC902

We are looking forward to see you there!

Meet and Greet Zoom Vol. 2

On Thursday, 18 February 2021, 3-5 pm

This meeting was designed to get to know each other and talk about general topics as well as the current research in the SFB. For this purpose, breakout sessions of 4-6 people were created. In the first part the following questions were discussed:

1. How did the current pandemic influence your work?

2. Where do you see yourself in the future?

3. What experiences did you make supervising interns?

The main part of the meeting was a power point karaoke where the students of the IRTG exchanged presentations and gave each other’s talks. The positive and non-threatening atmosphere during that session significantly enhanced the discussion during and after each talk.

We thank everyone for the participation and the great scientific exchange!

Guest Speaker – Julien Bethuné

On Thursday, 30.01.2020, 5.15 pm

Julien Bethuné (Heidelberg University Biochemistry Center), will give an SFB 902 lecture:

„Analysis of context-dependent protein complexes with next-generation proximity proteomics assays“.

Venue: TU Darmstadt, Campus Botanischer Garten, lecture hall: B101/52

Guests are welcome!


Since its initial description in 2012, the proximity-dependent biotinylation technique BioID has established itself as a reliable alternative to the classical Affinity Purification-MS approach for the identification of protein-protein interactions. Recently we engineering split-BioID, a proteinfragments complementation assay that greatly enhances the resolution of BioID by allowing the analysis of context-dependent protein complexes. Applied to the miRNA silencing pathway, split-BioID let us identify the 4EHP-binding protein GIGYF2 as a novel miRISC-associated factor. The 4EHPGIGYF2 dimer has been proposed to be recruited by RNA-binding proteins to stimulate the repression of translation of their associated transcripts. In line with this model we found that the
miRISC component TNRC6 directly binds to GIGYF2 which in turns promotes miRNA-mediated translation repression. More recently we uncovered an additional mechanism of GIGYF2-mediated repression that is independent of 4EHP but rather relies on the CCR4-NOT deadenylation complex. This suggests that GIGYF2 is part of two distinct functional units that exert distinct modes of repression on their associated target mRNAs. To define the composition of these context-dependent GIGYF2 complexes, we have developed more versatile proximity labeling assays that rely on a smaller labeling enzyme with improved labeling kinetics and that can be used in a split assay format.