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The structural plasticity of SCA7 domains defines their differential nucleosome‐binding properties
Author(s) -
Bonnet Jacques,
Wang YingHui,
Spedale Gianpiero,
Atkinson R Andrew,
Romier Christophe,
Hamiche Ali,
Pijnappel W W M Pim,
Timmers H Th Marc,
Tora László,
Devys Didier,
Kieffer Bruno
Publication year - 2010
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2010.98
Subject(s) - biology , nucleosome , coactivator , chromatin , microbiology and biotechnology , genetics , acetylation , zinc finger , histone , histone acetyltransferase , dna , transcription factor , gene
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.