Eukaryotic translation initiation factor 5A and its posttranslational modifications play an important role in proliferation and potentially in differentiation of the human enteric protozoan parasite Entamoeba histolytica
Fig 2
Multiple alignment of E. histolytica DHS and eIF5A protein sequences.
Conserved residues are marked by asterisks (*). Sequence alignment was performed using ClustalW. (A) Amino acid sequence alignment of E. histolytica DHS isoforms. Accession numbers of these sequences are as follows: EhDHS1 (XP_653614), EhDHS2 (XP_653426). The catalytic lysine residue is shown in red background, whereas NAD+ and spermidine binding sites are shown in green and yellow background, respectively. (B) Amino acid sequence alignment of E. histolytica eIF5A isoforms. Accession numbers of these sequences are as follows: EheIF5A1 (XP_657374); EheIF5A2 (XP_651531). The conserved lysine residues which are expected to be hypusinated are highlighted in red. Residues which are post-transnationally modified by acetylation and sulfation in human eIF5A, are shown in grey and cyan background, respectively.