Protein acetylation is one of the most frequent post-transcriptional modifications in eukaryotic cells and bacteria. Although the molecular bases of its action are not fully understood, it has been established that acetylation modulates important cellular processes such as the modification of chromatin structure, transcription, cell cycle progression, regulation of energy metabolism and microtubules dynamics. In many cases, acetylation generates a site of interaction between proteins, through an acetylated lysine recognition motif called the bromodomain (BD). This domain is the only known structural motif with specificity to recognize and bind acetylated lysines and has been exclusively described in nuclear proteins. Trypanosoma cruzi has seven BD-containing proteins designated TcBDF1 through TcBDF7, two of which are non-nuclear.

The general objective of the research line is to study the existence of nuclear and extranuclear bromodomain proteins in T. cruzi that participate in the modulation of different cellular events mediated by acetylation as potential points of intervention in the biology of the parasite to develop new chemotherapy drugs. In particular, we are studying the role of these proteins and acetylation itself in DNA transcription and repair, in the dynamics of the cytoskeleton, and during the infection and differentiation process.