Supplementary Figure 1: Experimental assay.
From: The bacterial cell division proteins FtsA and FtsZ self-organize into dynamic cytoskeletal patterns
(a) Illustration of protein interactions lipids (adapted from ref. 20): FtsA and ZipA bind to same highly conserved C-tail of FtsZ (shown in green), which is connected to the rest of the protein by a flexible linker.FtsA binds to the membrane surface using an amphipathix helix, located at the end of a C-terminal flexible linker. ZipA is a transmembrane protein. The N-terminal transmembrane-domain has been substituted by a His-tag obtaining His-Δ22-ZipA, which was then permanently attached to the membrane using Ni2+ chelating. (b) Commassie-stained SDS-Page gel of purified proteins used for this study. (c) Schematic drawing of the experimental assay. A plastic ring was glued to a glass cover slip to create a reaction chamber and a supported lipid bilayer was formed on the glass surface. FtsA, FtsZ and ATP were added to the buffer before polymerization of FtsZ was initiated by adding GTP.
