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Étude structurale de l'assemblage du complexe télomérique humain TRF2/RAP1

Abstract : Telomeres are the ends of eukaryotic linear chromosomes. They are made oftandem repeats of a short guanine-rich motif and bound by specific proteins.In vertebrates, these proteins form a complex called shelterin, theintegrity of which is critical to ensure proper replication of chromosomeends and to protect them against illicit targeting by DNA double-strandbreak repair pathways. Telomere dysfunctions lead to genome instability,which can ultimately cause senescence or cancer. Telomeres are a subnuclearregion in which shelterin proteins are highly enriched, enhancing lowaffinity interactions of important biological function. Among shelterinproteins, telomeric repeat-binding protein TRF2 and its constitutive partnerRAP1 are the main factors responsible for end protection. We studied indetails the assembly of TRF2/RAP1 complex by means of integrated structural,biophysical and biochemical approaches. We showed that this assemblydisplays important conformational adjustments of both proteins, and involvesa low affinity interaction engaging large regions in both proteins whichaffects their interaction properties.
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Guillaume Gaullier. Étude structurale de l'assemblage du complexe télomérique humain TRF2/RAP1. Biologie structurale [q-bio.BM]. Université Paris Sud - Paris XI, 2015. Français. ⟨NNT : 2015PA114831⟩. ⟨tel-01281310⟩

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