文献类型：期刊文献

英文题名：Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation

作者：Chen, Guochao[1];Wang, Duo[1,2];Wu, Bin[3];Yan, Fuxiang[1,2];Xue, Hongjuan[3];Wang, Quanmeng[4];Quan, Shu[5];Chen, Yong[1,6]

机构：[1]Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, Natl Ctr Prot Sci Shanghai, Ctr Excellence Mol Cell Sci,State Key Lab Mol Bio, Shanghai 200031, Peoples R China;[2]Univ Chinese Acad Sci, Beijing 100049, Peoples R China;[3]Chinese Acad Sci, Shanghai Adv Res Inst, Zhangjiang Lab, Natl Facil Prot Sci Shanghai, Shanghai 201210, Peoples R China;[4]Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Wuhan 430070, Peoples R China;[5]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, Shanghai 200237, Peoples R China;[6]ShanghaiTech Univ, Sch Life Sci & Technol, Shanghai 201210, Peoples R China

年份：2020

卷号：11

期号：1

外文期刊名：NATURE COMMUNICATIONS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:000569766000032)】；

基金：We thank the staff members of the Large-scale Protein Preparation System, the Integrated Laser Microscopy System, and the Nuclear Magnetic Resonance System at the National Facility for Protein Science Shanghai (NFPS) for providing technical support. We thank Jinqiu Zhou for the yeast strains and vectors, Zhongjun Qin for yeast CRISPRCas9 plasmids. This work was supported by grants from the Strategic Priority Research Program of the Chinese Academy of Sciences (XDB37010303 to Y.C.), the National Natural Science Foundation of China (31670748 and 31970576 to Y.C.), and the National Natural Science Foundation of China (31661143021 to S.Q.).

语种：英文

摘要：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(ET)) 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(ET), in a mechanism common to YEATS-associated ET domains (e.g., AF9(ET)) but not Bromo-associated ET domains from BET-family proteins. Thus, beyond identifying the molecular mechanism by which Taf14(ET) 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.S. cerevisiae TBP associated factor 14 (Taf14) is a transcriptional regulator that interacts with multiple nuclear complexes. Here, the authors report that the extra-terminal domain of Taf14 (Taf14(ET)) recognizes a common motif in various transcriptional coactivator proteins and they solve the NMR structure of Taf14(ET) bound the ET-binding motif of Sth1, the catalytic subunit of the RSC (Remodel the Structure of Chromatin) complex, and furthermore show that Taf14(ET) undergoes liquid-liquid phase separation, which is enhanced by Taf14 interaction partners.