The domain structure of Entamoeba alpha-actinin2

• Autorzy: Addario B. , Backman L.
• Języki publikacji: EN

Abstrakty

EN

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.

• Wydawca: -
• Czasopismo: Cellular and Molecular Biology Letters
• Rocznik: 2010
• Tom: 15
• Numer: 4
• Opis fizyczny: p.665-678,fig.,ref.

Twórcy

autor

Addario B.

• Department of Chemistry, Biochemistry, Umea University, SE-901 87 Umea, Sweden

autor

Backman L.

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