News from the Institute

As the German Research Foundation (DFG) announced today, Goethe University (GU) is one of the winners of the 2016 Competition for International Research Marketing Ideas.

In the latest issue of Cell, a team around IBC2 director Ivan Dikic reveals molecular details of a novel ubiquitination mechanism that may affect numerous life processes.

Earlier this year, U.S. colleagues reported that Legionella enzyme SdeA is capable of catalysing ubiquitination single-handedly. Now, the Frankfurt scientists together with collaborators from the MPI for Biology of Ageing (Cologne) have elucidated the chemistry behind and discovered a hitherto unknown type of linkage between ubiquitin and target proteins.

Genomic instability is a hallmark of cancer and aging. Scientists at Goethe University Frankfurt now discovered the molecular cause for genetic instability in patients suffering from a rare segmental progeroid syndrome named Ruijs-Aalfs syndrome. The syndrome leads to premature aging and early onset liver cancer.
“Until now, it was unclear how these patients, carrying mutations in the metalloprotease SPRTN, succumb to the disease”, comments Ivan Dikic, director of the Institute of Biochemistry II.

Raman et al. demonstrate transient SUMO-dependent complex formation between the AAA ATPase MDN1 and PELP1 during 60S biogenesis. They show that SUMO conjugation to PELP1 recruits MDN1 to pre-60S particles, while reversal of this modification by SENP3 is needed for the release of both factors during mammalian pre-ribosome remodeling.

The SUMO Signaling Group of IBCII find that SUMO signaling in hypoxia is altered by inactivation of SUMO-specific isopeptidases. Using proteomic analysis, we define a subset of hypoxia-induced SUMO1 targets and propose that hypoxia-induced SUMOylation of the transcriptional co- repressor BHLHE40 contributes to metabolic reprogramming under these conditions.