The structural plasticity of SCA7 domains defines their differential nucleosome‐binding properties |
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| Authors: | Gianpiero Spedale R Andrew Atkinson Christophe Romier Ali Hamiche W W M Pim Pijnappel H Th Marc Timmers László Tora Didier Devys Bruno Kieffer |
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| Affiliation: | 1. Department of Physiological Chemistry, University Medical Center Utrecht, Universiteitsweg 100, Utrecht, 3584 CG The Netherlands;2. Department of Structural Biology and Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U 964, Université de Strasbourg, BP 10142‐67404 Illkirch, France;3. Department of Functional Genomics and Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U 964, Université de Strasbourg, BP 10142‐67404 Illkirch, France |
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| Abstract: | SAGA (Spt–Ada–Gcn5 acetyltransferase), a coactivator complex involved in chromatin remodelling, harbours both histone acetylation and deubiquitination activities. ATXN7/Sgf73 and ATXN7L3, two subunits of the SAGA deubiquitination module, contain an SCA7 domain characterized by an atypical zinc‐finger. We show that the yeast Sgf73–SCA7 domain is not required to recruit Sgf73 into SAGA. Instead, it binds to nucleosomes, a property that is conserved in the human ATXN7–SCA7 domain but is lost in the ATXN7L3 domain. The solution structures of the SCA7 domain of both ATXN7 and ATXN7L3 reveal a new, common zinc‐finger motif at the heart of two distinct folds, providing a molecular basis for the observed functional differences. |
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| Keywords: | SAGA ATXN7 ubiquitin zinc‐finger nucleosome |
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