کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1979178 | 1061665 | 2011 | 8 صفحه PDF | دانلود رایگان |

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.
► SAGA is a 21-subunit transcriptional coactivator with multiple functions, including histone deubiquitination and acetylation.
► Structures of the SAGA deubiquitinating module (DUBm) show the four subunits, Ubp8, Sgf11, Sus1 and Sgf73 to form an unusual intertwined complex.
► Sus1 plays a conserved structural role in both the DUB module and the TREX-2 complex, which is involved in mRNA export.
► Structures of SCA7 of ATXN7 (human Sgf73) and the Tudor domains of Sgf29 provide new insights into SAGA recruitment.
Journal: Current Opinion in Structural Biology - Volume 21, Issue 6, December 2011, Pages 767–774