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

Type Article
Date 2021-02
Language English
Author(s) Alpha-Bazin Béatrice1, Gorlas Aurore2, Lagorce Arnaud2, 3, Joulié Damien1, Boyer Jean-Baptiste1, Dutertre Murielle2, Gaillard Jean-Charles1, Lopes Anne2, Zivanovic Yvan2, Dedieu Alain1, Confalonieri Fabrice2, Armengaud Jean1
Affiliation(s) 1 : Université Paris-Saclay, CEA, INRAE, Département Médicaments et Technologies pour la Santé (DMTS), SPI, 30200 Bagnols-sur-Cèze, France.
2 : Université Paris-Saclay, CEA, CNRS, Institute for Integrative Biology of the Cell (I2BC), 91198 Gif-sur-Yvette, France
3 : IHPE, Université de Montpellier, CNRS, Ifremer, Université de Perpignan, Via Domitia, Perpignan, France.
Source Journal Of Proteomics (1874-3919) (Elsevier BV), 2021-02 , Vol. 232 , P. 104044 (11p.)
DOI 10.1016/j.jprot.2020.104044
WOS© Times Cited 9
Keyword(s) Proteome, Post-translational modification, Acetylome, Archaea, Histone

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 is rather small, T. gammatolerans may enhance its toolbox by post-translational modification of its proteins. Here, we explored its extent of Nε-acetylation of lysines. For this, we immunopurified with two acetylated-lysine antibodies the acetylated peptides resulting from a proteolysis of soluble proteins with trypsin. The comparison of acetylated proteomes of two archaea highlights some common acetylation patterns but only 4 out of 26 orthologous proteins found to be acetylated in both species, are acetylated on the same lysine site. We evidenced that histone B is acetylated in T. gammatolerans at least at two different sites (K27 and K36), and a peptide common at the C-terminus of histones A and B is also acetylated. We verified that acetylation of histones is a common trait among Thermococcales after recording data on Thermococcus kodakaraensis histones and identifying three acetylated sites. This discovery reinforces the strong evolutionary link between Archaea and Eukaryotes and should be an incentive for further investigation on the extent and role of acetylation of histones in Archaea.


Acetylation is an important post-translational modification of proteins that has been extensively described in Eukaryotes, and more recently in Bacteria. Here, we report for the first time ever that histones in Archaea are also modified by acetylation after a systematic survey of acetylated peptides in Thermococcus gammatolerans. Structural models of histones A and B indicates that acetylation of the identified modified residues may play an important role in histone assembly and/or interaction with DNA. The in-depth protein acetylome landscape in T. gammatolerans includes at least 181 unique protein sequences, some of them being modified on numerous residues. Proteins involved in metabolic processes, information storage and processing mechanisms are over-represented categories in this dataset, highlighting the ancient role of this protein post-translational modification in primitive cells.

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Alpha-Bazin Béatrice, Gorlas Aurore, Lagorce Arnaud, Joulié Damien, Boyer Jean-Baptiste, Dutertre Murielle, Gaillard Jean-Charles, Lopes Anne, Zivanovic Yvan, Dedieu Alain, Confalonieri Fabrice, Armengaud Jean (2021). Lysine-specific acetylated proteome from the archaeon Thermococcus gammatolerans reveals the presence of acetylated histones. Journal Of Proteomics, 232, 104044 (11p.). Publisher's official version : , Open Access version :