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Identification and cellular localization of the actin‐binding protein ABP‐120 from Entamoeba histolytica
Author(s) -
Vargas Miguel,
Sansonetti Philippe,
Guillén Nancy
Publication year - 1996
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1996.01535.x
Subject(s) - entamoeba histolytica , biology , dictyostelium discoideum , spectrin , actin binding protein , actin , open reading frame , peptide sequence , binding protein , binding domain , cytoskeleton , biochemistry , amino acid , microbiology and biotechnology , gene , binding site , actin cytoskeleton , genetics , cell
Several actin‐binding proteins participate in the morphological changes that occur during amoeboid movement. The gene encoding one of these proteins, the gelation factor ABP‐120, was identified and characterized from trophozoites of Entamoeba histolytica . The sequence contains 2574 nucleotides, with an open reading frame of 858 amino acids, giving a protein of 93 kDa belonging to the spectrin family. The N‐terminal domain of ABP‐120 from E. histolytica revealed a consensus site for actin binding homologous to the actin‐binding sites of ABP‐120 of Dictyostelium discoideum , α‐actinin and spectrin. Analysis of the central domain revealed the presence of four repeats of a 73‐amino‐acid motif constituting 31% of the protein. In addition, a stretch of 105 amino acids was highly divergent when compared with the C‐terminal domain of D. discoideum ABP‐120. This sequence showed short motifs that are homologous to microtubule‐binding domains. We found that ABP‐120 from E. histolytica binds to F‐actin. In addition, upon motility of the parasite, this protein localized in the pseudopod and the uroid region, implying a role for ABP‐120 in movement and capping of surface receptors in E. histolytica .