IngentaConnect Identification and cellular localization of the actin-binding pro...

Authors: Vargas, Miguel¹; Sansonetti, Philippe¹; Guillén, Nancy¹

Source: Molecular Microbiology, Volume 22, Number 5, December 1996 , pp. 849-857(9)

Abstract:

Several actin-binding proteins participate in the morphological changes that occur during amoeboid movement. The gene encoding one of these proteins, the gelation factor ABP-120, was identified and characterized from trophozoites of Entamoeba histolytica. The sequence contains 2574 nucleotides, with an open reading frame of 858 amino acids, giving a protein of 93 kDa belonging to the spectrin family. The N-terminal domain of ABP-120 from E. histolytica revealed a consensus site for actin binding homologous to the actin-binding sites of ABP-120 of Dictyostelium discoideum, α-actinin and spectrin. Analysis of the central domain revealed the presence of four repeats of a 73-amino-acid motif constituting 31% of the protein. In addition, a stretch of 105 amino acids was highly divergent when compared with the C-terminal domain of D. discoideum ABP-120. This sequence showed short motifs that are homologous to microtubule-binding domains. We found that ABP-120 from E. histolytica binds to F-actin. In addition, upon motility of the parasite, this protein localized in the pseudopod and the uroid region, implying a role for ABP-120 in movement and capping of surface receptors in E. histolytica.

Document Type: Research article

DOI: 10.1046/j.1365-2958.1996.01535.x

Affiliations: 1: Unité de Pathogénie Microbienne Moléculaire, Institut National de la Santé et de la Recherche Médicale U389, Institut Pasteur, 28 Rue du Dr Roux, 75724 Paris Cédex 15, France.

The full text electronic article is available for purchase. You will be able to download the full text electronic article after payment.

$50.39 plus tax Refund Policy

Identification and cellular localization of the actin-binding protein ABP-120 from Entamoeba histolytica