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<dc:title xml:lang="en">Structural and functional studies of the BCL7 proteins : novel subunits of the mammalian SWI/SNF complex</dc:title>
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<dc:subject xml:lang="fr">Remodelage de la chromatine</dc:subject>
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<dc:subject xml:lang="en">Chromatin remodeling</dc:subject>
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<dcterms:abstract xml:lang="fr">Les protéines BCL7 sont de nouvelles sous-unités centrales récemment identifiées du complexe de remodelage de la chromatine dépendant de l'ATP SWI/SNF chez les mammifères. Les mutations des protéines BCL7 sont associées à différents types de cancers. Les informations sur la fonction moléculaire et sur la structure des protéines BCL7 sont à ce jour très limitées. En utilisant des approches biochimiques et structurelles, ce projet visait à mieux comprendre la structure et la fonction de ces sous-unités auxiliaires. Nous rapportons ici que les protéines BCL7 se lient directement à la particule centrale du nucléosome (NCP) et à l'ADN libre avec une haute affinité, formant des complexes bien définis avec la NCP. Nous caractérisons en outre l'impact des mutations de la protéine BCL7 signalées chez les patients atteints de cancer sur la liaison avec la NCP</dcterms:abstract>
<dcterms:abstract xml:lang="en">Epigenetic regulation of the chromatin fiber involves the activity of ATP-dependent chromatin remodelers. BCL7 proteins are recently identified novel core subunits of the mammalian SWI/SNF ATP-dependent chromatin remodeler complex. Mutations in BCL7 proteins are associated with different kind of cancers including blood malignancies. The information on the molecular function and on the structure of BCL7 proteins is to date very limited. Using biochemical and structural approaches, this project aimed to gain insight into the structure and function of these auxiliary subunits. Here we report that BCL7 proteins bind directly the nucleosome core particle (NCP) and free DNA with high affinity, forming well defined complexes with the NCP. We further characterize the impact of BCL7 protein mutations reported in cancer patients on NCP binding.</dcterms:abstract>
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