title: The domain structure of Entamoeba α-actinin2.
abstract: Entamoeba histolytica, a major agent of human amoebiasis, expresses two distinct forms of α-actinin, a ubiquitous actin-binding protein that is present in most eukaryotic organisms. In contrast to all metazoan α-actinins, in both isoforms the intervening rod domain that connects the N-terminal actin-binding domain with the C-terminal EF-hands is much shorter. It is suggested that these α-actinins may be involved in amoeboid motility and phagocytosis, so we cloned and characterised each domain of one of these α-actinins to better understand their functional role. The results clearly showed that the domains have properties very similar to those of conventional α-actinins.
authors.affiliation: Department of Chemistry, Umeå University, Sweden.
authors.forename: Barbara
authors.initials: B
authors.lastname: Addario
authors.forename: Lars
authors.initials: L
authors.lastname: Backman
mesh_terms: D000185:Actinin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000595:Amino Acid Sequence; D004747:Entamoeba / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011487:Protein Conformation
chemical_list: D000199:Actins; D010455:Peptides; D000185:Actinin