Fil: Ochaya, Stephen. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Respuela, Patricia. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.Fil: Simonsson, Maria. Ludwig Institute for Cancer Research; Suecia.Fil: Saraswathi, Abhiman. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Branche, Carole. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Lee, Jennifer. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Bua, Jacqueline. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Nilsson, Daniel. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Fil: Åslund, Lena. Rudbeck Laboratory. Department of Genetics and Pathology; Suecia.Fil: Bontempi, Esteban. ANLIS Dr.C.G.Malbrán. Instituto Nacional de Parasitología; Argentina.Fil: Andersson, Björn. Karolinska Institutet. Department of Cell and Molecular Biology; Suecia.Trypanosomatids are widespread parasites that cause three major tropical diseases. In trypanosomatids, as in most other organisms, acetylation is a common protein modification that is important in multiple, diverse processes. This paper describes a new member of the Trypanosoma cruzi acetyltransferase family. The gene is single copy and orthologs are also present in the other two sequenced trypanosomatids, Trypanosoma brucei and Leishmania major. This protein (TcAT-1) has the essential motifs present in members of the GCN5-related acetyltransferase (GNAT) family, as well as an additional motif also found in some enzymes from plant and animal species. The protein is evolutionarily more closely related to this group of enzymes than to histone acetyltransferases. The native protein has a cytosolic cellular location and is present in all three life-cycle stages of the parasite. The recombinant protein was shown to have autoacetylation enzymatic activity.