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

Guochao Chen, Duo Wang, Bin Wu, Fuxiang Yan, Hongjuan Xue, Quanmeng Wang, Shu Quan and Yong Chen ()
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Guochao Chen: Chinese Academy of Sciences
Duo Wang: Chinese Academy of Sciences
Bin Wu: Chinese Academy of Sciences
Fuxiang Yan: 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

Nature Communications, 2020, vol. 11, issue 1, 1-14

Abstract: 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.

Date: 2020
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DOI: 10.1038/s41467-020-18021-7

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