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. © 2010 Versita Warsaw and Springer-Verlag Wien.
CITATION STYLE
Addario, B., & Backman, L. (2010). The domain structure of Entamoeba α-actinin2. Cellular and Molecular Biology Letters, 15(4), 665–678. https://doi.org/10.2478/s11658-010-0035-z
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