CV Science

Sylvain Daujat PhD Health and Biology, Montpellier, France

Course and current status

2000: PhD from University of Montpellier II, directed by Dr. Jacques Piette at the IGMM, MONTPELLIER, FRANCE : Role of the oncoprotein Mdm2, one of the main regulator of the tumor suppressor p53, during early mouse development.

2001 – 2004: Post-doc CRUK in the group of Prof. Tony Kouzarides at the Wellcome Trust/Cancer Research UK/Gurdon Institute, CAMBRIDGE, UK: Role of histone arginine methylation in chromatin and transcriptional regulation.

2005 – 20011: project leader as a Max-Planck researcher in the group of Dr. Robert Schneider at the Max-Planck Institute for Immunobiology and Epigenetics, FREIBURG, GERMANY: understand the role of histone modifications in the regulation of DNA-dependent activities, focusing on new players with the linker histone H1 and the globular domain of the core histone H3.

20012 – present: INSERM researcher and project leader in epigenetics at the Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC) on the role on a new class of histone modifications located in the core of the nucleosome in the regulation of chromatin functions and gene expression.

Scientific summary

The epigenetic regulation of genome function is now recognized as a fundamental principle of cellular activity. It allows us to understand how genetic information can be differentially expressed both spatially and temporally. The covalent modification of histones affects chromatin dynamics and participates in the remodelling of chromatin, ensuring the plasticity required for the proper expression of our genes. Understanding how this works mechanistically and identifying new modifications that could extend our knowledge remain major challenges in the field. 

Most of the research in the chromatin field has been focused on the N-terminal tail modification of core histones. Very little was known about modifications and their physiological significance within the histone globular domains, which have long been regarded only as structural scaffolds for nucleosome formation. In addition, N-terminal histone modifications fulfil their role in chromatin dynamics and transcriptional regulation indirectly through the activity of binding partners called effectors. Some amino acids that map to nucleosome regions in close proximity to the DNA, called the octamer lateral surface, can be post-translationally modified. These residues on the lateral surface can make direct or indirect contact with the DNA, and modifications of these particular residues have the potential to alter DNA-histone interaction and hence regulate nucleosomal mobility and/or stability and chromatin dynamics. 

Therefore deciphering the interplay and role of such modifications is essential considering the fact that they can alter DNA–histone interactions within and between nucleosomes, thereby potentially affecting higher order chromatin structures and essential process such as cell proliferation, development and disease.