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Structure of SAGA and mechanism of TBP deposition on gene promoters

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  • Gabor Papai

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

  • Alexandre Frechard

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

  • Olga Kolesnikova

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

  • Corinne Crucifix

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

  • Patrick Schultz

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

  • Adam Ben-Shem

    (Institut de Génétique et de Biologie Moléculaire et Cellulaire, Integrated Structural Biology Department, Equipe labellisée Ligue Contre le Cancer
    Centre National de la Recherche Scientifique, UMR7104
    Institut National de la Santé et de la Recherche Médicale
    Université de Strasbourg)

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 nucleate the pre-initiation complex on DNA, a pivotal event in the expression of protein-encoding genes1. 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.

Suggested Citation

  • Gabor Papai & Alexandre Frechard & Olga Kolesnikova & Corinne Crucifix & Patrick Schultz & Adam Ben-Shem, 2020. "Structure of SAGA and mechanism of TBP deposition on gene promoters," Nature, Nature, vol. 577(7792), pages 711-716, January.
  • Handle: RePEc:nat:nature:v:577:y:2020:i:7792:d:10.1038_s41586-020-1944-2
    DOI: 10.1038/s41586-020-1944-2
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    Cited by:

    1. Ke Chen & Li Wang & Zishuo Yu & Jiali Yu & Yulei Ren & Qianmin Wang & Yanhui Xu, 2024. "Structure of the human TIP60 complex," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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