Additional file 2: Figure S1. of Segregation of prokaryotic magnetosomes organelles is driven by treadmilling of a dynamic actin-like MamK filament

Alignment of actins ATPase motifs and magnetosome chain parameters: mean-squared displacement, apparent diffusion constant and velocity. (A) The Connect 1 and Phosphate 2 motif from the ATPase domain [72] were aligned from several prokaryotic actins and the human actin. Red residues indicate high conservation. The residues of the MSR MamK protein, glutamate E143 and aspartate D161, mutated in this work are indicated. Alignment was performed in CLC Main Workbench software as per Derman et al. [9] using the following sequences: MSR MamK (CAM78025.1), AMB MamK (WP_011383398.1), E. coli ParM (WP_000959884.1), Bacillus subtillis MreB (WP_003229650.1), B. subtillis AlfA (WP_013603336.1), B. subtillis Alp7A (WP_013603291.1), Homo sapiens Actin (NP_001605.1). (B) Magnetosome chain (MC) mean-squared displacement (MSD) as a function of time in the wildtype (WT) (n = 24) and mamK D161A (n = 19) strains. MSD was determined from the MamC-EGFP fluorescence signal. (C) MC apparent diffusion constant (D*) as a function of time calculated from MSD data. (D) MC velocity (VMC) determined from displacement data (time interval: 10 min) for the WT and mamK D161A strains. (PDF 141 kb)