FtsZ rings (green) in E. coli cells stained for DNA (blue) observed by 3D-SIM
Welcome to the Margolin Lab!
A cell is like a city, with an organized yet dynamic infrastructure grouped into specialties. For the last 28 years, my lab has investigated how the simplest cells—bacteria—organize themselves and divide to make progeny cells. We mainly focus on how bacteria such as E. coli achieve the daunting task of splitting themselves in two at just the right time (once their genetic material is duplicated) and place (exactly in the middle) every 20 minutes without making errors. The keys to this success are ancient and universal versions of protein polymers of actin (FtsA) and tubulin (FtsZ), which our lab visualized for the first time in living bacteria over 20 years ago. Today, we use state of the art super-resolution imaging, combined with molecular genetics, protein biochemistry, interaction studies, and in vitro reconstitution, to gain more detailed insights into the structure and regulation of these cytoskeletal polymers and their associated proteins, which comprise the dynamic membrane-associated protein nanomachine (divisome) that divides bacterial cells. Thanks in part to our characterization of bypass suppressors of essential divisome proteins, it is now becoming clear that the divisome is highly flexible and can remodel itself in response to various inputs and perturbations. Despite impressive contributions by many labs, there is much to be learned about overall divisome structure, the interchangeability of its parts, and how it remodels in response to temporal and environmental cues.