What an ancient bacterial cytoskeletal protein can teach us about dissipative self-assembly

Biological systems offer a large showcase of self-assembling structures constituted from a variety of materials (lipids, proteins, nucleic acids, to name a few). Most challenging is understanding one its most intriguing modalities: dissipative self-assembly. Continuous conversion of energy stored in chemical fuels, such as ATP or GTP allows generating dynamic complex structures that can self-heal and adapt to changing environments. Great progress has been made in developing synthetic chemically driven systems that mimic some of the features present in nature. However, a deeper understanding of the dissipative self-assembly of the ancient bacterial cytoskeletal protein FtsZ, simpler than the more widely studied eukaryotic actin and tubulin, might help us get new insights. I will present out work carried out over the last years trying to understand, from single filament analysis in reconstituted systems, theoretical modelling, and, more recently, single molecule fluorescence measurements, how FtsZ, an essential soluble protein responsible for bacterial cell division orchestrates such an essential function after associating and assembling on the cell membrane.