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Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex

Author

Listed:
  • Minh Chau Nguyen

    (University of Colorado School of Medicine)

  • Hosein Rostamian

    (The University of North Carolina School of Medicine
    The University of North Carolina School of Medicine)

  • Ana Raman

    (Johns Hopkins University School of Medicine)

  • Pengcheng Wei

    (National Jewish Health
    Guangxi University)

  • Dustin C. Becht

    (University of Colorado School of Medicine)

  • Annette H. Erbse

    (University of Colorado)

  • Brianna J. Klein

    (University of Colorado School of Medicine)

  • Tonya M. Gilbert

    (Johns Hopkins University School of Medicine)

  • Gongyi Zhang

    (National Jewish Health)

  • M. Andres Blanco

    (University of Pennsylvania, School of Veterinary Medicine)

  • Brian D. Strahl

    (The University of North Carolina School of Medicine)

  • Sean D. Taverna

    (Johns Hopkins University School of Medicine
    University of Arkansas for Medical Sciences)

  • Tatiana G. Kutateladze

    (University of Colorado School of Medicine)

Abstract

The NuA3 complex is a major regulator of gene transcription and the cell cycle in yeast. Five core subunits are required for complex assembly and function, but it remains unclear how these subunits interact to form the complex. Here, we report that the Taf14 subunit of the NuA3 complex binds to two other subunits of the complex, Yng1 and Sas3, and describe the molecular mechanism by which the extra-terminal domain of Taf14 recognizes the conserved motif present in Yng1 and Sas3. Structural, biochemical, and mutational analyses show that two motifs are sandwiched between the two extra-terminal domains of Taf14. The head-to-toe dimeric complex enhances the DNA binding activity of Taf14, and the formation of the hetero-dimer involving the motifs of Yng1 and Sas3 is driven by sequence complementarity. In vivo assays in yeast demonstrate that the interactions of Taf14 with both Sas3 and Yng1 are required for proper function of the NuA3 complex in gene transcription and DNA repair. Our findings suggest a potential basis for the assembly of three core subunits of the NuA3 complex, Taf14, Yng1 and Sas3.

Suggested Citation

  • Minh Chau Nguyen & Hosein Rostamian & Ana Raman & Pengcheng Wei & Dustin C. Becht & Annette H. Erbse & Brianna J. Klein & Tonya M. Gilbert & Gongyi Zhang & M. Andres Blanco & Brian D. Strahl & Sean D., 2024. "Molecular insight into interactions between the Taf14, Yng1 and Sas3 subunits of the NuA3 complex," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-49730-y
    DOI: 10.1038/s41467-024-49730-y
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    References listed on IDEAS

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    1. Guochao Chen & Duo Wang & Bin Wu & Fuxiang Yan & Hongjuan Xue & Quanmeng Wang & Shu Quan & Yong Chen, 2020. "Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation," Nature Communications, Nature, vol. 11(1), pages 1-14, December.
    2. Xiaobing Shi & Tao Hong & Kay L. Walter & Mark Ewalt & Eriko Michishita & Tiffany Hung & Dylan Carney & Pedro Peña & Fei Lan & Mohan R. Kaadige & Nicolas Lacoste & Christelle Cayrou & Foteini Davrazou, 2006. "ING2 PHD domain links histone H3 lysine 4 methylation to active gene repression," Nature, Nature, vol. 442(7098), pages 96-99, July.
    3. Brianna J. Klein & Jordan T. Feigerle & Jibo Zhang & Christopher C. Ebmeier & Lixin Fan & Rohit K. Singh & Wesley W. Wang & Lauren R. Schmitt & Thomas Lee & Kirk C. Hansen & Wenshe R. Liu & Yun-Xing W, 2022. "Taf2 mediates DNA binding of Taf14," Nature Communications, Nature, vol. 13(1), pages 1-11, December.
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