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A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection.

Abstract : 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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https://hal-pasteur.archives-ouvertes.fr/pasteur-00853764
Contributor : Melanie Hamon <>
Submitted on : Friday, August 23, 2013 - 3:04:20 PM
Last modification on : Friday, May 29, 2020 - 4:33:53 PM

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Haig A Eskandarian, Francis Impens, Marie-Anne Nahori, Guillaume Soubigou, Jean-Yves Coppée, et al.. A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection.. Science, American Association for the Advancement of Science, 2013, 341 (6145), pp.1238858. ⟨10.1126/science.1238858⟩. ⟨pasteur-00853764⟩

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