A new chapter in the transcription SAGA.
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.
Department of Biophysics and Biophysical Chemistry and the Howard Hughes Medical Institute, 725 N. Wolfe Street, Baltimore, MD 21205, USA.
Nadine L
NL
Samara
Cynthia
C
Wolberger
D000818:Animals; D001665:Binding Sites; D002843:Chromatin / Q000378:metabolism; D006801:Humans; D021122:Protein Subunits / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D013329:Structure-Activity Relationship; D015534:Trans-Activators / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D014158:Transcription, Genetic
D002843:Chromatin; D021122:Protein Subunits; D015534:Trans-Activators