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.
Highlights
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
We found that the bromodomain of Sth[1] (Sth11248–1359) did not interact with Taf14’s ET domain (Taf14ET), while the Sth[1] fragments comprising residues 1183–1240 and 1199–1225 were able to associate with Taf14ET (Fig. 1b)
The interaction between Taf14ET and Sth11183–1240 was further confirmed by isothermal titration calorimetry (ITC) (Fig. 1c)
Summary
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. We demonstrate that the extra-terminal (ET) domain of Taf[14] (Taf14ET) recognizes a common motif in multiple transcriptional coactivator proteins from several nuclear complexes, including RSC, SWI/SNF, INO80, NuA3, TFIID, and TFIIF. Consistent with its multifaceted functions, Taf[14] physically associates with more than seven transcriptionally relevant complexes, including the chromatin remodeling complexes SWI/SNF, INO80, and RSC, the acetyltransferase complex NuA3, the general transcription factors TFIID and TFIIF, and the mediator complex[6,7,8,9,10,11].
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