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Etude structurale du complexe de remodelage de la chromatine NuRD et sa sous-unité MBD3 liée à l'ADN

Abstract : Transcription regulation of chromatin is a very dynamic process regulated through the recruitment of chromatin-remodeling complexes. My work focuses on NuRD for Nucleosome remodeling and histones deacetylation complex a 1 MDa multi-subunit protein complex and its subunit MBD3 a CpG-binding protein and more precisely on an integrated biology approach of this molecular assembly and its interaction with DNA. It combines biochemical preparation, biophysical characterization, single particle cryo-eletron microscopy and x-ray crystallography. Biophysical analysis show that MBD domain of MBD3 interacts with unmodified CpG DNA, a crystal diffracting up to 3.9 Å were obtained. Moreover a C-terminal intrinsically disordered region of MBD3 were identified and despite is inherent disorder seems to increase the binding affinity of MBD3 for DNA. Crystals were obtained for both constructs in complex with DNA and are currently optimized.Cryo-EM study of NuRD complex allows us to develop and optimized purification and grids preparation for the visualization of the complex. The present results reveal a domain organization of the complex never identify before.
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Rachel Tabaroni. Etude structurale du complexe de remodelage de la chromatine NuRD et sa sous-unité MBD3 liée à l'ADN. Biophysique. Université de Strasbourg, 2018. Français. ⟨NNT : 2018STRAJ094⟩. ⟨tel-02918031⟩

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