TATA-box-binding protein / Subunit (17 kDa) of TFIID and SAGA complexes, involved in RNA polymerase II transcription initiation / Subunit (60 kDa) of TFIID and SAGA complexes / Transcription initiation factor TFIID subunit 10 / Ubiquitin carboxyl-terminal hydrolase / Transcription-associated protein / Uncharacterized protein / Subunit of SAGA histone acetyltransferase complex / Transcriptional coactivator HFI1/ADA1 / Transcriptional regulator involved in glucose repression of Gal4p-regulated genes ...TATA-box-binding protein / Subunit (17 kDa) of TFIID and SAGA complexes, involved in RNA polymerase II transcription initiation / Subunit (60 kDa) of TFIID and SAGA complexes / Transcription initiation factor TFIID subunit 10 / Ubiquitin carboxyl-terminal hydrolase / Transcription-associated protein / Uncharacterized protein / Subunit of SAGA histone acetyltransferase complex / Transcriptional coactivator HFI1/ADA1 / Transcriptional regulator involved in glucose repression of Gal4p-regulated genes / Transcription and mRNA export factor SUS1 / SAGA-associated factor 11 / Subunit of the SAGA and SAGA-like transcriptional regulatory complexes, interacts with Spt15p to act / Subunit (90 kDa) of TFIID and SAGA complexes / Subunit of the SAGA transcriptional regulatory complex, involved in proper assembly of the complex / BJ4_G0016160.mRNA.1.CDS.1 / Polyubiquitin-B / Polyubiquitin-B / Subunit (61/68 kDa) of TFIID and SAGA complexes
Journal: Nature / Year: 2020 Title: Structure of SAGA and mechanism of TBP deposition on gene promoters. Authors: Gabor Papai / Alexandre Frechard / Olga Kolesnikova / Corinne Crucifix / Patrick Schultz / Adam Ben-Shem / Abstract: SAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to ...SAGA (Spt-Ada-Gcn5-acetyltransferase) is a 19-subunit complex that stimulates transcription via two chromatin-modifying enzymatic modules and by delivering the TATA box binding protein (TBP) to nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes. Here we present the structure of yeast SAGA with bound TBP. The core of the complex is resolved at 3.5 Å resolution (0.143 Fourier shell correlation). The structure reveals the intricate network of interactions that coordinate the different functional domains of SAGA and resolves an octamer of histone-fold domains at the core of SAGA. This deformed octamer deviates considerably from the symmetrical analogue in the nucleosome and is precisely tuned to establish a peripheral site for TBP, where steric hindrance represses binding of spurious DNA. Complementary biochemical analysis points to a mechanism for TBP delivery and release from SAGA that requires transcription factor IIA and whose efficiency correlates with the affinity of DNA to TBP. We provide the foundations for understanding the specific delivery of TBP to gene promoters and the multiple roles of SAGA in regulating gene expression.
M: TATA-binding protein A: Transcriptional coactivator HFI1/ADA1 C: Subunit of SAGA histone acetyltransferase complex F: Spt20 D: Subunit of the SAGA and SAGA-like transcriptional regulatory complexes, interacts with Spt15p to act E: Subunit of the SAGA transcriptional regulatory complex, involved in proper assembly of the complex J: Transcription initiation factor TFIID subunit 10 K: Subunit (61/68 kDa) of TFIID and SAGA complexes G: Subunit (90 kDa) of TFIID and SAGA complexes H: Subunit (60 kDa) of TFIID and SAGA complexes I: Subunit (17 kDa) of TFIID and SAGA complexes, involved in RNA polymerase II transcription initiation L: Transcription-associated protein B: Transcriptional regulator involved in glucose repression of Gal4p-regulated genes N: Spt8 R: Polyubiquitin-B Q: Ubiquitin carboxyl-terminal hydrolase O: SAGA-associated factor 11 P: Transcription and mRNA export factor SUS1
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