Silvia Domcke & Valentin Flury
Maryline Minoux
Gabriele Fontana & Daniel Hess receive their Prize from Susan Gasser, the FMI Director



October 5, 2018

Congratulations to the FMI Prize winners 2018

As in previous years, several internal prizes were awarded during the FMI Annual Meeting, a 3 day scientific meeting attended by most scientists in the institute. This year the Annual Meeting took place in Pontresina, in the Swiss Alps. The prizes are the Ed Fischer Prize for the best thesis, the Max M. Burger Prize for the most outstanding postdoctoral publication, and the Chiquet Prize for an original discovery. Learn more about this year’s winners.

Ed Fischer Prize

Silvia Domcke (Schübeler group) and Valentin Flury (Bühler group) were both awarded the Ed Fisher Prize 2018 for outstanding theses in 2017. The prize is named after Ed Fischer who was awarded the Nobel Prize in Medicine in 1992 and who was for many years on the Scientific Advisory Board of the FMI.

Silvia Domcke is interested in understanding gene regulation and how it gives rise to cell type-specific gene expression patterns. For her PhD she investigated the role of DNA methylation, an epigenetic mark, in this process. Silvia and collaborators could show that DNA methylation guides a specific subset of transcription factors to their correct genomic locations. It also serves to prevent deleterious transcription factor binding and transcriptional activation of endogenous retroviruses, which are found throughout the genome.

Valentin Flury investigated how chromatin states are initiated and maintained, studying the fission yeast Schizosaccharomyces pombe. Valentin and collaborators discovered a self-reenforcing feedback loop acting in euchromatin that prevents unwanted heterochromatin formation. This is the first characterization of a euchromatic feedback loop that counteracts better characterized feedback loops in heterochromatin. It suggests that feedback loops are generally important to ensure correct gene expression and to maintain specific chromatin states.

» See the list of previous Ed Fischer Prize winner

Max M.Burger Prize

Marilyne Minoux (Rijli group) was awarded the Max M.Burger Prize 2018, which recognizes an outstanding paper by a postdoctoral fellow in 2017. This prize is named after Max Burger who was Director of the FMI for almost 15 years (1987-2001).

In a study published in Science, Maryline discovered an epigenetic mechanism that regulates cranial-facial morphogenesis.

Neural crest cells – the cells that give rise to the various facial structures – arise from the neural tube and migrate into the craniofacial region to provide most of the skull and face cartilages and bones. The 'positional' identity that the neural crest cells acquire in order to generate the appropriate head skeletal structures is established after migration, through differential cell-cell contacts. Even then, the positional identity of the neural crest cells is not irreversibly fixed and they maintain plasticity. Maryline identified a specific set of epigenetic chromatin marks that allow neural crest cells to maintain their plasticity through early development, preserving  their potential to express the range of position-specific transcriptional programs that give rise to the chin, cheekbones or forehead.

» Read more about this paper
» Learn more about Maryline and her work
» See the list of previous Max M. Burger Prize winners

Chiquet-Ehrismann Originality Prize

Gabriele Alessandro Fontana (Rass group) and Daniel Hess (Proteomics and Protein Analysis facility) are the co-recipients of the Chiquet-Ehrismann Prize 2018. This award is named after the late Ruth Chiquet-Ehrismann who was a group leader at the FMI from 1985 to 2015. She was successful at pursuing non-mainstream topics that nonetheless had major biomedical impact.

Proteins are targets of many post-translational modifications that regulate their functions in a temporal and spatial manner. Among those modifications is lipidation, through which hydrophobic fatty acids are covalently attached to the polypeptide. This increases the affinity of proteins for cellular membranes. While several oncoproteins are known lipidation targets, it has not yet been possible to map the sites at which proteins are modified. Gabriele and Daniel developed a robust, highly-sensitive method to map lipidation sites in vivo, facilitating future studies aimed at investigating the functional consequences of protein lipidations in both physiological and pathological situations.

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