The domain structure of Entamoeba α-actinin2
2010 (English)In: Cellular & Molecular Biology Letters (Druk), ISSN 1425-8153, E-ISSN 1689-1392, Vol. 15, no 4, 665-78 p.Article in journal (Refereed) Published
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.
Place, publisher, year, edition, pages
Springer , 2010. Vol. 15, no 4, 665-78 p.
α-actinin, Spectrin repeat, Actin-binding protein
IdentifiersURN: urn:nbn:se:umu:diva-36544DOI: 10.2478/s11658-010-0035-zISI: 000282175000011PubMedID: 20865366OAI: oai:DiVA.org:umu-36544DiVA: diva2:354673