Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation
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 (Taf14ET) recognizes a common motif in various transcriptional coactivator proteins and they solve the NMR st...
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Nature Portfolio
2020
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oai:doaj.org-article:5199bb852e6d4eb29c3b0d7f59cc88812021-12-02T18:01:13ZTaf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation10.1038/s41467-020-18021-72041-1723https://doaj.org/article/5199bb852e6d4eb29c3b0d7f59cc88812020-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-18021-7https://doaj.org/toc/2041-1723S. 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 (Taf14ET) recognizes a common motif in various transcriptional coactivator proteins and they solve the NMR structure of Taf14ET bound the ET-binding motif of Sth1, the catalytic subunit of the RSC (Remodel the Structure of Chromatin) complex, and furthermore show that Taf14ET undergoes liquid-liquid phase separation, which is enhanced by Taf14 interaction partners.Guochao ChenDuo WangBin WuFuxiang YanHongjuan XueQuanmeng WangShu QuanYong ChenNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-14 (2020) |
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Science Q Guochao Chen Duo Wang Bin Wu Fuxiang Yan Hongjuan Xue Quanmeng Wang Shu Quan Yong Chen Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
description |
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 (Taf14ET) recognizes a common motif in various transcriptional coactivator proteins and they solve the NMR structure of Taf14ET bound the ET-binding motif of Sth1, the catalytic subunit of the RSC (Remodel the Structure of Chromatin) complex, and furthermore show that Taf14ET undergoes liquid-liquid phase separation, which is enhanced by Taf14 interaction partners. |
format |
article |
author |
Guochao Chen Duo Wang Bin Wu Fuxiang Yan Hongjuan Xue Quanmeng Wang Shu Quan Yong Chen |
author_facet |
Guochao Chen Duo Wang Bin Wu Fuxiang Yan Hongjuan Xue Quanmeng Wang Shu Quan Yong Chen |
author_sort |
Guochao Chen |
title |
Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
title_short |
Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
title_full |
Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
title_fullStr |
Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
title_full_unstemmed |
Taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
title_sort |
taf14 recognizes a common motif in transcriptional machineries and facilitates their clustering by phase separation |
publisher |
Nature Portfolio |
publishDate |
2020 |
url |
https://doaj.org/article/5199bb852e6d4eb29c3b0d7f59cc8881 |
work_keys_str_mv |
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1718378987815698432 |