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

EMBO Reports
Jacques BonnetBruno Kieffer

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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Citations

Mar 20, 2012·Genes & Development·Gianpiero SpedaleW W M Pim Pijnappel
Oct 13, 2012·Critical Reviews in Biochemistry and Molecular Biology·Amparo Galán, Susana Rodríguez-Navarro
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Jul 4, 2020·Experimental & Molecular Medicine·Youngseo CheonDaeyoup Lee
Jun 20, 2020·European Journal of Neurology : the Official Journal of the European Federation of Neurological Societies·M G BahC Mignot
Feb 11, 2014·The Journal of Biological Chemistry·Christian KoehlerBruno Kieffer
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Aug 3, 2020·Biochimica Et Biophysica Acta. Gene Regulatory Mechanisms·Dominique HelmlingerLászló Tora
May 15, 2021·Cancer Letters·Tingting FengXiao Xu

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