A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection.
2013
Eskandarian, Haig A | Impens, Francis | Nahori, Marie-Anne | Soubigou, Guillaume | Coppée, Jean-Yves | Cossart, Pascale | Hamon, Mélanie A | Interactions Bactéries-Cellules (UIBC) ; Institut National de la Recherche Agronomique (INRA)-Institut Pasteur [Paris] (IP)-Institut National de la Santé et de la Recherche Médicale (INSERM) | INSERM ; Institut National de la Santé et de la Recherche Médicale (INSERM) | Department of Medical Protein Research (VIB) ; Vlaams Instituut voor Biotechnologie | Department of Biochemistry ; Universiteit Gent = Ghent University = Université de Gand (UGENT) | Transcriptome et Epigénome (PF2) ; Institut Pasteur [Paris] (IP) | Work in the Cossart laboratory is funded by the Pasteur Institute, Inserm (U604), Institut National de la Recherche Agronomique (USC2020), the Fondation Louis Jeantet, the European Research Council (advanced grant 233348 MODELIST), the Fondation Le Roch Les Mousquetaires, and the Agence Nationale pour la Recherche grants (ERANET "LISTRESS" and EPILIS)
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Show more [+] Less [-]English. Pathogens dramatically affect host cell transcription programs for their own profit during infection, but in most cases, the underlying mechanisms remain elusive. We found that during infection with the bacterium Listeria monocytogenes, the host deacetylase sirtuin 2 (SIRT2) translocates to the nucleus, in a manner dependent on the bacterial factor InlB. SIRT2 associates with the transcription start site of a subset of genes repressed during infection and deacetylates histone H3 on lysine 18 (H3K18). Infecting cells in which SIRT2 activity was blocked or using SIRT2(-/-) mice resulted in a significant impairment of bacterial infection. Thus, SIRT2-mediated H3K18 deacetylation plays a critical role during infection, which reveals an epigenetic mechanism imposed by a pathogenic bacterium to reprogram its host.
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