Glycosomal Bromodomain Factor 1 from Trypanosoma cruzi enhances trypomastigotes cell infection and intracellular amastigotes growth.

RITAGLIATI C; VILLANOVA GV; ALONSO VL; ARAUJO ZUMA A; CRIBB P; MACHADO MOTTA, MC; SERRA EC

BIOCHEMICAL JOURNAL

PORTLAND PRESS LTD

Lugar: Londres; Año: 2015

0264-6021

Acetylation is a ubiquitous protein modification present in prokaryotic and eukaryotic cells that participates in the regulation of many cellular processes. The bromodomain is the only domain known to bind acetylated lysines. In the last years many bromodomain inhibitors have been developed in order to treat diseases caused by aberrant acetylation of lysine residues and have been tested as anti-parasitic drugs. Here, we report the first characterization of T. cruzi Bromodomain Factor 1. Tc BDF1 is expressed in all life cycle stages but it is developmentally regulated. It localizes in the glycosomes directed by a PTS2 sequence. The overexpression of Tc BDF1 wild type is detrimental for epimastigotes, but it enhances the infectivity rate of trypomastigotes and the replication of amastigotes. On the other hand, the overexpression of a mutated version of Tc BDF1 has no effect on epimastigotes, but it does negatively affect on trypomastigotes? infection and amastigotes? replication.