Anti-silencing factor 1 (ASF1) is a histone chaperone that contributes to the histone deposition during nucleosome assembly in newly replicated DNA. It is involved in chromatin disassembly, transcription activation and in the cellular response to DNA damage. In
Leishmania major
the ASF1 gene (
LmASF1) is located in chromosome 20 and codes for a protein showing 67% of identity with the Trypanosoma brucei
TbASF1a. Compared to orthologous proteins,
LmASF1 conserves the main residues relevant for its various biological functions. To study ASF1 in
Leishmania we generated a mutant overexpressing
LmASF1 in
L. major. We observed that the excess of
LmASF1 impaired promastigotes growth rates and had no impact on cell cycle progress. Differently from yeast, ASF1 overproduction in
Leishmania did not affect expression levels of genes located on telomeres, but led to an upregulation of proteins involved in chromatin remodelling and physiological stress, such as heat shock proteins, oxidoreductase activity and proteolysis. In addition, we observed that
LmASF1 mutant is more susceptible to the DNA damaging agent, methyl methane sulphonate, than the control line. Therefore, our study suggests that ASF1 from
Leishmania pertains to the chromatin remodelling machinery of the parasite and acts on its response to DNA damage.
