Fig. 1
From: Structural basis for membrane tethering by a bacterial dynamin-like pair
Biochemical purification and characterisation of Cj-DLP1 and Cj-DLP2. a Cartoon schematic providing nomenclature for dynamin family hinge 1 and hinge 2-mediated conformations. Many dynamin family members undergo large-scale conformational changes mediated by hinges 1 and 2 at the interface of trunk/neck or neck/G-domains, respectively. b cj-dlp1 and cj-dlp2 exist as a side-by-side gene pair within an operon that putatively includes an HcpA-like β-lactamase. c Alignment of Cj-DLP1 and Cj-DLP2 G1-G4 GTP binding motifs with other members of the dynamin family. Cj-DLP1 (Uniprot accession CJ0411), Cj-DLP2 (CJ0412), Nostoc punctiforme BDLP1 (B2IZD3), Bacillus subtilis (P54159), Escherichia coli LeoA (E3PN25), human Mitofusin 1 (Q8IWA4), human Mitofusin 2 (O95140), human OPA1 (O60313), Saccharomyces cerevisiae Fzo1p (P38297), human Dynamin 1 (Q05193). Consensus sequence is highlighted in blue. d Cj-DLP1 and Cj-DLP2 purify as 84.5 kDa and 71.2 kDa proteins, respectively, as shown by SDS–PAGE. e SEC-MALS shows that Cj-DLP1 and Cj-DLP2 are monomeric in solution but form a 2:2 stoichiometric tetramer, termed Cj-DLP1/2tetramer, when mixed (left panel). Corresponding SDS–PAGE Coomassie and SYPRO staining of Cj-DLP1/2tetramer with stoichiometry (right panel)
