SCA7 结构域的结构可塑性定义了它们与核小体的不同结合特性。
The structural plasticity of SCA7 domains defines their differential nucleosome-binding properties.
机构信息
Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire (IGBMC), CNRS UMR 7104, INSERM U 964, Université de Strasbourg, Illkirch, France.
出版信息
EMBO Rep. 2010 Aug;11(8):612-8. doi: 10.1038/embor.2010.98. Epub 2010 Jul 16.
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.
摘要
SAGA（SpT-Ada-Gcn5 乙酰转移酶）是一种参与染色质重塑的共激活复合物，具有组蛋白乙酰化和去泛素化活性。ATXN7/Sgf73 和 ATXN7L3 是 SAGA 去泛素化模块的两个亚基，它们含有一个 SCA7 结构域，其特征是一个非典型的锌指。我们表明，酵母 Sgf73-SCA7 结构域对于将 Sgf73 募集到 SAGA 中不是必需的。相反，它与核小体结合，这一特性在人类 ATXN7-SCA7 结构域中是保守的，但在 ATXN7L3 结构域中丢失了。ATXN7 和 ATXN7L3 的 SCA7 结构域的溶液结构揭示了两个不同折叠中心的一个新的、常见的锌指模体，为观察到的功能差异提供了分子基础。
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