Detection of the Endosomal Sorting Complex Required for Transport in Entamoeba histolytica and Characterization of the EhVps4 Protein
Figure 2
Comparison of EhVps4 with other Vps4 proteins. (a) Schematic representation of Vps4 proteins from human, yeast and E. histolytica. Conserved MIT, AAA, and Vps4 C-terminal (C) domains were predicted using PROSITE and Pfam programs. (b) Phylogenetic relationships between EhVps4 and homologous proteins from other organisms. The phylogenetic tree of Vps4 homologues was created with the MEGA 3.1 program using the Neighbor Joining algorithm based on ClustalW alignments of complete amino acids sequences. Numbers on tree nodes represent the bootstrap proportions (%) of 1000 replications. The UniProt KnowledgeBase database accession number for each protein is indicated before the organism. (c) Comparison of 3D structures of MIT and AAA domains from human (Hs), yeast (Sc) and E. histolytica (Eh) Vps4 homologues. 3D modeling of EhVps4 MIT and AAA domains was obtained using crystal data from yeast Vps4p MIT (2v6xA) and AAA (2qpaB) domains as template, respectively.
