6LQZ
Solution structure of Taf14ET-Sth1EBMC
Summary for 6LQZ
| Entry DOI | 10.2210/pdb6lqz/pdb |
| NMR Information | BMRB: 36309 |
| Descriptor | Transcription initiation factor TFIID subunit 14, Nuclear protein STH1/NPS1 (2 entities in total) |
| Functional Keywords | protein interaction module, phase separation, transcription |
| Biological source | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) More |
| Total number of polymer chains | 2 |
| Total formula weight | 14700.73 |
| Authors | |
| Primary citation | Chen, G.,Wang, D.,Wu, B.,Yan, F.,Xue, H.,Wang, Q.,Quan, S.,Chen, Y. Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation. Nat Commun, 11:4206-4206, 2020 Cited by PubMed 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 (Taf14) 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 Taf14, in a mechanism common to YEATS-associated ET domains (e.g., AF9) but not Bromo-associated ET domains from BET-family proteins. Thus, beyond identifying the molecular mechanism by which Taf14 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. PubMed: 32826896DOI: 10.1038/s41467-020-18021-7 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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