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Identification and characterization of HIRIP3 as a novel histone H2A chaperone

Abstract : The genome of eukaryotic cells is packaged into chromatin, which establishment and maintenance require mechanisms of assembly and remodelling. This thesis work was dedicated to the characterization of two factors of chromatin assembly machinery. The first factor studied in this work was HIRIP3, a mammalian homologue of yeast H2A.Z chaperone Chz1. We aimed to test whether HIRIP3 is a histone chaperone by itself. At first, we established HIRIP3 interaction with histones in vivo. After then, we studied the structural specificity of this interaction in vitro. We have characterized HIRIP3 as a novel H2A histone chaperone that utilizes the CHZ motif for its function. The second part of this work was focused on SRCAP chromatin remodelling complex. We aimed to decipher its interaction network and to describe its sub-complexes. We have reconstituted YL1, SRCAP, TIP49A, TIP49B and H2A.Z/H2B core complex using baculovirus expression system. Our protocol allowed us to purify core complex suitable for future structural studies by cryo-electron microscopy.
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Submitted on : Thursday, August 20, 2020 - 9:45:36 AM
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  • HAL Id : tel-02917943, version 1



Maria Ignatyeva. Identification and characterization of HIRIP3 as a novel histone H2A chaperone. Genomics [q-bio.GN]. Université de Strasbourg, 2017. English. ⟨NNT : 2017STRAJ028⟩. ⟨tel-02917943⟩



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