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The domain structure of Entamoeba α-actinin2

Addario, Barbara (author)
Umeå universitet,Kemiska institutionen
Backman, Lars (author)
Umeå universitet,Kemiska institutionen
 (creator_code:org_t)
Springer, 2010
2010
English.
In: Cellular & Molecular Biology Letters (Druk). - : Springer. - 1425-8153 .- 1689-1392. ; 15:4, s. 665-78
  • Journal article (peer-reviewed)
Abstract Subject headings
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  • 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.

Keyword

α-actinin
Spectrin repeat
Actin-binding protein

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