Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, 725 N. Wolfe Street, Baltimore, MD 21205, USA.
Curr Opin Struct Biol. 2011 Dec;21(6):767-74. doi: 10.1016/j.sbi.2011.09.004. Epub 2011 Oct 18.
Eukaryotic transcriptional coactivators are multi-subunit complexes that both modify chromatin and recognize histone modifications. Until recently, structural information on these large complexes has been limited to isolated enzymatic domains or chromatin-binding motifs. This review summarizes recent structural studies of the SAGA coactivator complex that have greatly advanced our understanding of the interplay between its different subunits. The structure of the four-protein SAGA deubiquitinating module has provided a first glimpse of the larger organization of a coactivator complex, and illustrates how interdependent subunits interact with each other to form an active and functional enzyme complex. In addition, structures of the histone binding domains of ATXN7 and Sgf29 shed light on the interactions with chromatin that help recruit the SAGA complex.
真核转录共激活因子是多亚基复合物,既能修饰染色质,又能识别组蛋白修饰。直到最近,这些大型复合物的结构信息还仅限于分离的酶结构域或染色质结合基序。本综述总结了 SAGA 共激活因子复合物的最新结构研究,这些研究极大地促进了我们对其不同亚基之间相互作用的理解。四蛋白 SAGA 去泛素化模块的结构首次提供了对共激活因子复合物更大组织的了解,并说明了相互依赖的亚基如何相互作用形成一个活跃和功能的酶复合物。此外,ATXN7 和 Sgf29 的组蛋白结合域结构揭示了有助于招募 SAGA 复合物的与染色质的相互作用。