MOBIRISE

Molecular pathways are often highly complex with specific mechanisms being governed by multiple protein-protein interactions and protein-lipid interactions, and further regulated by enzymatic activities such as ATP or GTP hydrolysis. We take a reductionist approach to investigate each biochemical event in vitro. With an ever-expanding library of purified proteins and lipids we employ a combination of classical biochemical, biophysical and high resolution microscopic techniques to investigate specific molecular events. Recently, we have been investigating the polar oscillation of the Min system, direct interactions between FtsZ, FtsA and the lipid bilayer, and targeting and degradation of antitoxins, including MqsA, and cell division proteins by the AAA+ proteases ClpXP and Lon... FtsZ is a highly conserved bacterial cell division protein that is a structural homolog of tubulin and polymerizes to form a dynamic protein structure called the "Z-ring" at midcell. At the Z-ring, the center..