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The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties

The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties,10.1038/embor.2010.98,Embo Reports,Jacques Bonnet,Y

The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties   (Citations: 5)
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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.
Journal: Embo Reports - EMBO REP , vol. 11, no. 8, pp. 612-618, 2010
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