Post-Doc in Biochemistry (M/F)

id="offer-description" class="ecl-u-type-heading-2 ecl-u-mt-none ecl-u-mb-l">Offer Description Iron-sulfur (Fe-S) clusters are essential and ubiquitous small protein metallocofactors acting in diverse cellular functions including ATP production, biosynthesis of metabolites, gene expression, DNA repair and signaling. These cofactors cannot be acquired from external sources, they must be synthesized de novo by multi-proteins machineries. Fe-S cluster biogenesis is tightly linked to cellular metabolism. In eukaryotes, Fe-S cluster biogenesis by the ISC machinery is regulated by fatty acid synthesis (FASII pathway) via the acyl carrier protein (ACP). Fatty acids are precursors for membrane phospholipids and lipopolysaccharides, as well as for essential cofactors, including biotin and lipoic acid. Conversely, Fe-S cluster enzymes are tightly linked to fatty acids: the respiratory chain producing ATP integrates lipids and several membrane Fe-S cluster enzymes, biotin and lipoic acids synthesis require Fe-S cluster enzymes and acetyl-CoA, the substrate for the generation of fatty acids is also a substrate for the Krebs cycle which relies on the Fe-S cluster enzyme aconitase. Recent data from the laboratory point to a regulation of Fe-S cluster biogenesis by the FASII pathway in prokaryotes via direct interaction of ACP with the ISC machinery, but via a completely different mechanism compared to eukaryotes. The goal of this project is to elucidate the biochemical mechanism connecting