Publisher Correction: Active matter in space.
NPJ microgravity 9:1 (2023) 18
Non-reciprocal multifarious self-organization.
Nature nanotechnology 18:1 (2023) 79-85
Abstract:
A hallmark of living systems is the ability to employ a common set of building blocks that can self-organize into a multitude of different structures. This capability can only be afforded in non-equilibrium conditions, as evident from the energy-consuming nature of the plethora of such dynamical processes. To achieve automated dynamical control of such self-assembled structures and transitions between them, we need to identify the fundamental aspects of non-equilibrium dynamics that can enable such processes. Here we identify programmable non-reciprocal interactions as a tool to achieve such functionalities. The design rule is composed of reciprocal interactions that lead to the equilibrium assembly of the different structures, through a process denoted as multifarious self-assembly, and non-reciprocal interactions that give rise to non-equilibrium dynamical transitions between the structures. The design of such self-organized shape-shifting structures can be implemented at different scales, from nucleic acids and peptides to proteins and colloids.Dependence of diffusion in Escherichia coli cytoplasm on protein size, environmental conditions, and cell growth.
eLife 11 (2022) e82654
Abstract:
Inside prokaryotic cells, passive translational diffusion typically limits the rates with which cytoplasmic proteins can reach their locations. Diffusion is thus fundamental to most cellular processes, but the understanding of protein mobility in the highly crowded and non-homogeneous environment of a bacterial cell is still limited. Here, we investigated the mobility of a large set of proteins in the cytoplasm of Escherichia coli, by employing fluorescence correlation spectroscopy (FCS) combined with simulations and theoretical modeling. We conclude that cytoplasmic protein mobility could be well described by Brownian diffusion in the confined geometry of the bacterial cell and at the high viscosity imposed by macromolecular crowding. We observed similar size dependence of protein diffusion for the majority of tested proteins, whether native or foreign to E. coli. For the faster-diffusing proteins, this size dependence is well consistent with the Stokes-Einstein relation once taking into account the specific dumbbell shape of protein fusions. Pronounced subdiffusion and hindered mobility are only observed for proteins with extensive interactions within the cytoplasm. Finally, while protein diffusion becomes markedly faster in actively growing cells, at high temperature, or upon treatment with rifampicin, and slower at high osmolarity, all of these perturbations affect proteins of different sizes in the same proportions, which could thus be described as changes of a well-defined cytoplasmic viscosity.Efficiency of navigation strategies for active particles in rugged landscapes
Frontiers in Physics Frontiers 10 (2022) 1034267
Active matter in space.
NPJ microgravity 8:1 (2022) 54