Lysine-specific acetylated proteome from the archaeon Thermococcus gammatolerans reveals the presence of acetylated histones

Thermococcus gammatolerans EJ3 is an extremophile archaeon which was revealed as one of the most radioresistant organisms known on Earth, withstanding up to 30 kGy gamma-ray radiations. While its theoretical proteome rather small, T. may enhance toolbox by post-translational modification proteins. Here, we explored extent N?-acetylation lysines. For this, immunopurified with two acetylated-lysine antibodies acetylated peptides resulting from a proteolysis soluble proteins trypsin. The comparison proteomes archaea highlights some common acetylation patterns but only 4 out 26 orthologous found be in both species, are same lysine site. We evidenced that histone B at least different sites (K27 and K36), peptide C-terminus histones A also acetylated. verified trait among Thermococcales after recording data kodakaraensis identifying three sites. This discovery reinforces strong evolutionary link between Archaea Eukaryotes should incentive for further investigation role Archaea. Acetylation important has been extensively described Eukaryotes, more recently Bacteria. report first time ever modified systematic survey gammatolerans. Structural models indicates identified residues play assembly and/or interaction DNA. in-depth protein acetylome landscape includes 181 unique sequences, them being numerous residues. Proteins involved metabolic processes, information storage processing mechanisms over-represented categories this dataset, highlighting ancient primitive cells.