Trypanosoma cruzi Bromodomain Factor 2 (BDF2) binds to acetylated histones and is accumulated after UV irradiation

VILLANOVA, GABRIELA VANINA; NARDELLI, SHEILA CRISTINA; CRIBB, PAMELA; MAGDALENO, ANAHÍ; SILBER, ARIEL MARIANO; MOTTA, MARIA CRISTINA M.; SCHENKMAN, SERGIO; SERRA, ESTEBAN

INTERNATIONAL JOURNAL FOR PARASITOLOGY

Elsevier

Año: 2009 vol. 39 p. 665 - 673

0020-7519

Histone tails post-translational modifications (acetylation, methylation, phosphorylation, ubiquitination, and ADP-ribosylation) regulate many cellular processes. Among these modifications, phosphorylation, methylation and acetylation have been already described in trypanosomatid histones. Bromodomains, together with chromodomains and histone-binding SANT domains, were proposed to be responsible for the “histone code” reading. Trypanosoma cruzi genome encodes four CDSs that contain a bromodomain, named TcBDF1-4. Here we showed that one of them, TcBDF2, is expressed in discrete regions inside the nucleus of all the parasite life cycle stages and binds H4 and H2A purified histones from T. cruzi. Immunolocalization experiments using both anti-histone H4 acetylated peptides and anti-TcBDF2 antibodies, determined that TcBDF2 co-localizes with histone H4 acetylated at lysines K10 and K14. TcDBF2 and K10 acetylated H4 interaction was confirmed by co-immunoprecipitation It is also shown that TcBDF2 was accumulated after UV irradiation in T. cruzi epimastigotes. These results suggest that TcBDF2 could be taking part of a chromatin remodelling complex in T. cruzi.