Adenylate kinase 1 (TzADK1) in Trypanosoma cruzi.

BOUVIER, LEON; MIRANDA, MARIANA; CANEPA, GASPAR; PEREIRA, CA

Rosario

Congreso; XLII Reunión anual Sociedad Argentina de Investigación Bioquímica y Biología Molecular (SAIB); 2006

Adenylate kinases are phosphotransferases, which catalyze the interconversion of adenosine nucleotides. These enzymes maintain the cellular ATP homeostasis and duplicate ATP´s energetic potential. While eukaryotic cells typically contain three adenylate kinase isoforms, kinetoplastid parasites present at least three additional isoenzymes. The unusual large amount of adenilate kinase variants present in these organisms is explained by their differential intracellular positioning. In this way each variant presents particular structural characteristics which account for their localization. In Trypanosoma cruzi TzADK1 is an isoform with a particular long N-terminal domain. This enzyme is homologous to TbADKA from Trypanosoma brucei, which has been shown to be targeted to the flagellum. In this work we study the localization of TzAdK1 and the association to cellular structures by means of Western-Blot and the expression of GFP-fusion proteins in Trypanosoma cruzi. Other adenylate kinase isoforms were also characterized.