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  • Research Article
  • Open Access

The domain structure of Entamoeba α-actinin2

Cellular & Molecular Biology LettersAn International Journal201015:35

https://doi.org/10.2478/s11658-010-0035-z

  • Received: 2 April 2010
  • Accepted: 10 September 2010
  • Published:

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.

Key words

  • α-actinin
  • Spectrin repeat
  • Actin-binding protein

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