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Etude structurale et fonctionnelle de la variante d'histone H2AZ

Abstract : The histone variant H2AZ has emerged as a key regulator of chromatin function and plays an essential role in transcriptional activation, cell proliferation, development, and differentiation. H2AZ marks nucleosomes flanking the promoters of most genes, but the mechanistic basis for this localization is unknown. A mechanistic understanding of nucleosome assembly/disassembly requiresa detailed knowledge of nucleosome thermodynamics and histone chaperones. The aim of my thesis was to identify specific chaperone involved in H2AZ dynamic by using biochemical and proteomic strategies. To elucidate the mechanism of H2AZ deposition/eviction, I purified the prenucelosomal H2AZ complex and characterized in details the interacting protein partners. I found that Anp32e is a member of the presumed H2A.Z histone-exchange complex p400/TIP60. Bacterially expressed Anp32e binds only to the H2AZ/H2B dimers but not to the H2A/H2B. Anp32e interacts with a short region of the docking domain of H2A.Z. The binding occurred through a novel Anp32e motif, termed ZID. Finally, I show that down regulation of Anp32e interferes with both the de-repression of hormone dependent genes and H2A.Z removal from their promoter. Our data identified Anp32e as a novel mammalian H2AZ chaperone invoved in H2AZ eviction.
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Submitted on : Monday, December 2, 2013 - 1:12:08 AM
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Arnaud Obri. Etude structurale et fonctionnelle de la variante d'histone H2AZ. Biochimie, Biologie Moléculaire. Université de Strasbourg, 2012. Français. ⟨NNT : 2012STRAJ097⟩. ⟨tel-00912335⟩

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