Characterization of entamoeba histolytica alpha-actinin
2006 (English)In: Molecular and biochemical parasitology (Print), ISSN 0166-6851, E-ISSN 1872-9428, Vol. 145, no 1, 11-17 p.Article in journal (Refereed) Published
We have cloned, expressed and characterized a alpha-actinin-like protein of Entamoeba histolytica. Analysis of the primary structure reveals that the essential domains of the alpha-actinin protein family are conserved: an N-terminus actin-binding domain, a C-terminus calcium-binding domain and a central helical rod domain. However, the rod domain of this Entamoeba protein is considerably shorter than the rod domain in alpha-actinins of higher organisms. The cloned Entamoeba 63 kDa protein is recognized by conventional alpha-actinin antibodies as well as binds and cross-links filamentous actin and calcium ions in the same manner as alpha-actinins. Despite the shorter rod domain this protein has conserved the most important functions of alpha-actinins. Therefore, it is suggested that this 63 kDa protein is an atypical and ancestral alpha-actinin.
Place, publisher, year, edition, pages
Amsterdam: Elsevier/North-Holland , 2006. Vol. 145, no 1, 11-17 p.
Actinin/chemistry/genetics/metabolism, Actins/metabolism, Animals, Calcium/metabolism, Circular Dichroism, Cloning; Molecular, Entamoeba histolytica/*metabolism/ultrastructure, Microscopy; Electron; Transmission, Sequence Analysis; DNA, Spectrometry; Mass; Matrix-Assisted Laser Desorption-Ionization/methods
IdentifiersURN: urn:nbn:se:umu:diva-12341DOI: doi:10.1016/j.molbiopara.2005.09.003PubMedID: 16219372OAI: oai:DiVA.org:umu-12341DiVA: diva2:152012