Bonnet J, et al. (2010) The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties. EMBO Rep 11(8):612-8
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.
|Status: Published||Type: Journal Article||PubMed ID: 20634802|
Topics addressed in this paper
Number of different genes curated to this paper: 22
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|Topics||Genes linked to topics (#1 - 10 )|
|Fungal Related Genes/Proteins|
|Non-Fungal Related Genes/Proteins|
|Protein Sequence Features|
|Protein-Nucleic Acid Interactions|
|Topics||Genes linked to topics (#11 - 20 )|
|Topics||Genes linked to topics (#21 - 22 )|