Extended Data Fig. 1: Sequence alignment and predicted protein structures.
From: NSF/αSNAP2-mediated cis-SNARE complex disassembly precedes vesicle fusion in Arabidopsis cytokinesis
(a) Alignment of C-terminal sequences of αSNAP-related proteins. Arabidopsis thaliana αSNAP1 (AT3G56450) and αSNAP2 (AT3G56190) were aligned with αSNAP from human (Homo sapiens, GenBank NP_003818), cattle (Bos taurus, GenBank AAB25812) and yeast (Saccharomyces cerevisiae, GenBank NP_009503) in the CLC Main Workbench program. Note that αSNAP1 is larger than the other αSNAPs and less similar to bovine αSNAP (E value 1e-29 vs. 2e-71 for αSNAP2). Asterisk marks the conserved leucine residue L288 that was mutated to alanine in this study. Numbers indicate protein lengths (amino acid residues). (b-e) Structural models of NSF and αSNAP2. Predicted structures of wild type NSF (grey, b and c) and αSNAP2 (grey, d and e) are superimposed with those of dominant-negative NSFEQ (green, b and c) and αSNAP2LA (blue, d and e), respectively. The substituted residues are highlighted in red (b-e). (c and e) Boxed areas in (b and d) at higher magnification.
