MemProDx · The dynamic structure of protein domains within the cytoplasmic membrane of Escherichia coli

Membrane proteins govern how bacteria inside the human body, animals, plants, water sources or soil interact with their environment. Membrane proteins show intricate spatial organization and can be compartmentalized in the membrane, but it is unknown how they dynamically assemble and vanish from membrane domains. In this project, I aim to reveal the dynamic organization of membrane protein domains in the inner membrane of Escherichia coli. I will examine the distribution and dynamics of proteins that engage in protein domains and play crucial roles in the distribution of other proteins in the membrane. These proteins are responsible for functions like membrane protein translocation, quality control, lipid raft formation, and synthesis of the peptidoglycan scaffold. By employing live-cell super-resolution and single-molecule fluorescence imaging, I will observe the assembly, movement, and variations in size and content of protein domains within growing bacterial cells. I will investigate the impact of external conditions like heat- and osmotic stress, starvation, and antibiotics on the dynamics of membrane protein domains. This proposal addresses a fundamental gap in our understanding of the organization of proteins in bacterial membranes and thus offers insights into various processes from chemotaxis to pathogen-host interactions. The development of super-resolution fluorescence microscopy protocols for imaging membrane proteins in live bacterial cells will be a methodological achievement, enabling further advancements in the field.