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Project #6721
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#6721 : Regulation of Sirtuin 2-dependent histone deacetylation during bacterial infection
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Name of Applicant : Jorge Pereira
Date of application : 04-07-2016
Unit : Chromatin and Infection
Location : Roux (53) > Rez de chaussée > 05
Phone : 0144389318
@ Mail : jorge.pereira@pasteur.fr
@ PI-Mail : melanie.hamon@pasteur.fr

Project context and summary :

One of the best models for the study of bacteria-host interactions is Listeria monocytogenes. One interesting facet of this bacterium is its ability to modify host chromatin. Recently, we have shown that Listeria causes a drastic deacetylation of histone H3 on lysine 18 (H3K18dc). Interestingly, to impose this modification, Listeria highjacks previously undescribed host machinery: the host protein sirtuin 2 (SIRT2) is relocalized to the nucleus where it causes genes repression during infection. SIRT2 is a NAD-dependent deacetylase that has been implicated in the regulation of complex processes such as aging and cancer. This protein had been mainly studied in the cytoplasm, and although SIRT2 had been show to shuttle between the cytoplasm and the nucleus, the mechanism and its biological role remained unknown.        In order to further characterize the role of SIRT2 during infection and identify all the genes at which it is recruited, we are performing ChIP-seq analysis. These studies are expected to bring new insights into the function and regulation of SIRT2 by characterizing this new phosphorylation site.


Related team publications :
Eskandarian, H.A., Impens, F., Nahori, M.-A., Soubigou, G., Coppe´ e, J.-Y., Cossart, P., and Hamon, M.A. (2013). A role for SIRT2-dependent histone H3K18 deacetylation in bacterial infection. Science 341, 1238858.
Jorge M. Pereira, Hamon, M.A., Cossart, P., 2016. A Lasting Impression : Epigenetic Memory of Bacterial Infections ? Cell Host Microbe 579–582. doi:10.1016/j.chom.2016.04.012
Service Delivery
Project Manager : claudia.chica@pasteur.fr
Project Type : Short
Status : Closed
Global Satisfaction for this application : Pretty Good (4/5)


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