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Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation

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  • Guochao Chen

    (Chinese Academy of Sciences)

  • Duo Wang

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Bin Wu

    (Chinese Academy of Sciences)

  • Fuxiang Yan

    (Chinese Academy of Sciences
    University of Chinese Academy of Sciences)

  • Hongjuan Xue

    (Chinese Academy of Sciences)

  • Quanmeng Wang

    (Huazhong Agricultural University)

  • Shu Quan

    (East China University of Science and Technology)

  • Yong Chen

    (Chinese Academy of Sciences
    ShanghaiTech University)

Abstract

Saccharomyces cerevisiae TBP associated factor 14 (Taf14) is a well-studied transcriptional regulator that controls diverse physiological processes and that physically interacts with at least seven nuclear complexes in yeast. Despite multiple previous Taf14 structural studies, the nature of its disparate transcriptional regulatory functions remains opaque. Here, we demonstrate that the extra-terminal (ET) domain of Taf14 (Taf14ET) recognizes a common motif in multiple transcriptional coactivator proteins from several nuclear complexes, including RSC, SWI/SNF, INO80, NuA3, TFIID, and TFIIF. Moreover, we show that such partner binding promotes liquid-liquid phase separation (LLPS) of Taf14ET, in a mechanism common to YEATS-associated ET domains (e.g., AF9ET) but not Bromo-associated ET domains from BET-family proteins. Thus, beyond identifying the molecular mechanism by which Taf14ET associates with many transcriptional regulators, our study suggests that Taf14 may function as a versatile nuclear hub that orchestrates transcriptional machineries to spatiotemporally regulate diverse cellular pathways.

Suggested Citation

  • 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.
  • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18021-7
    DOI: 10.1038/s41467-020-18021-7
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    Cited by:

    1. 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.
    2. 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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