Characterization of Entamoeba histolytica alpha-actinin.
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.
Virel
Ana
A
Biochemistry, Umeå University, SE-901 87 Umeå, Sweden.
Backman
Lars
L
D000185:Actinin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D002942:Circular Dichroism; D003001:Cloning, Molecular; D004748:Entamoeba histolytica / Q000378:metabolism* / Q000648:ultrastructure; D046529:Microscopy, Electron, Transmission; D017422:Sequence Analysis, DNA; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization / Q000379:methods
D000199:Actins; D000185:Actinin; D002118:Calcium