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Journal Articles EMBO Reports Year : 2010

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

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.

Dates and versions

hal-03465202 , version 1 (03-12-2021)

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Jacques Bonnet, Ying‐hui Wang, Gianpiero Spedale, R Andrew Atkinson, Christophe Romier, et al.. The structural plasticity of SCA7 domains defines their differential nucleosome‐binding properties. EMBO Reports, 2010, 11 (8), pp.612-618. ⟨10.1038/embor.2010.98⟩. ⟨hal-03465202⟩
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