Fig. 6
From: Structural basis for membrane tethering by a bacterial dynamin-like pair
Cj-DLP1/2tetramer binds, tubulates and tethers liposomes in trans. a Spin assays show that only Cj-DLP1/2tetramer binds lipid efficiently at low (0.5 µM) concentration. The addition of nucleotide has no obvious effect. Removal of the Cj-DLP1 trunks to create Cj-DLP1∆trunk/DLP2tetramer inhibits lipid binding. S = supernatant, P = pellet. b SEC-MALS shows that mixing of Cj-DLP1∆trunk and Cj-DLP2 maintains a Cj-DLP1/2tetramer-like assembly. c Cj-DLP1, Cj-DLP2 and Cj-DLP1/2tetramer bind and tubulate lipid at high protein concentration (≥10 µM). Tube morphology appears overall similar across all samples and irrespective of nucleotide addition. Scale bar = 200 nm. d Dynamic light scattering plot shows significant Cj-DLP1/2tetramer-mediated liposome tethering or fusion. Tethering is not observed with Cj-DLP1∆trunk/DLP2tetramer. e Fluorescent microscopy shows that only Cj-DLP1/2tetramer is competent to induce liposome tethering or fusion. Scale bar = 10 µM. Inset panel = 4 µM. f Cartoon model showing the mechanism of nucleotide free Cj-DLP1/2tetramer-mediated liposome tethering at low concentration (0.5 µM)
