A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing
In fission yeast, Erh1, ortholog of human ERH, interacts with the YTH family RNA binding protein Mmi1 to form the Erh1-Mmi1 complex (EMC), which has been implicated in gene silencing. Here, the authors present the cocrystal structure of Erh1 homodimers interacting with Mmi1 and further characterise...
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Format: | Article |
Language: | English |
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Nature Portfolio
2019-01-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/s41467-018-08273-9 |
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author | Guodong Xie Tommy V. Vo Gobi Thillainadesan Sahana Holla Beibei Zhang Yiyang Jiang Mengqi Lv Zheng Xu Chongyuan Wang Vanivilasini Balachandran Yunyu Shi Fudong Li Shiv I. S. Grewal |
author_facet | Guodong Xie Tommy V. Vo Gobi Thillainadesan Sahana Holla Beibei Zhang Yiyang Jiang Mengqi Lv Zheng Xu Chongyuan Wang Vanivilasini Balachandran Yunyu Shi Fudong Li Shiv I. S. Grewal |
author_sort | Guodong Xie |
collection | DOAJ |
description | In fission yeast, Erh1, ortholog of human ERH, interacts with the YTH family RNA binding protein Mmi1 to form the Erh1-Mmi1 complex (EMC), which has been implicated in gene silencing. Here, the authors present the cocrystal structure of Erh1 homodimers interacting with Mmi1 and further characterise the role of EMC in facultative heterochromatin assembly and gene silencing. |
first_indexed | 2024-12-17T18:53:58Z |
format | Article |
id | doaj.art-4e751db81f374d0581b9e726b90ed9a9 |
institution | Directory Open Access Journal |
issn | 2041-1723 |
language | English |
last_indexed | 2024-12-17T18:53:58Z |
publishDate | 2019-01-01 |
publisher | Nature Portfolio |
record_format | Article |
series | Nature Communications |
spelling | doaj.art-4e751db81f374d0581b9e726b90ed9a92022-12-21T21:36:24ZengNature PortfolioNature Communications2041-17232019-01-0110111510.1038/s41467-018-08273-9A conserved dimer interface connects ERH and YTH family proteins to promote gene silencingGuodong Xie0Tommy V. Vo1Gobi Thillainadesan2Sahana Holla3Beibei Zhang4Yiyang Jiang5Mengqi Lv6Zheng Xu7Chongyuan Wang8Vanivilasini Balachandran9Yunyu Shi10Fudong Li11Shiv I. S. Grewal12Hefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of HealthLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of HealthLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of HealthHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of HealthHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaHefei National Laboratory for Physical Sciences at the Microscale, School of Life Sciences, University of Science and Technology of ChinaLaboratory of Biochemistry and Molecular Biology, National Cancer Institute, National Institutes of HealthIn fission yeast, Erh1, ortholog of human ERH, interacts with the YTH family RNA binding protein Mmi1 to form the Erh1-Mmi1 complex (EMC), which has been implicated in gene silencing. Here, the authors present the cocrystal structure of Erh1 homodimers interacting with Mmi1 and further characterise the role of EMC in facultative heterochromatin assembly and gene silencing.https://doi.org/10.1038/s41467-018-08273-9 |
spellingShingle | Guodong Xie Tommy V. Vo Gobi Thillainadesan Sahana Holla Beibei Zhang Yiyang Jiang Mengqi Lv Zheng Xu Chongyuan Wang Vanivilasini Balachandran Yunyu Shi Fudong Li Shiv I. S. Grewal A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing Nature Communications |
title | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing |
title_full | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing |
title_fullStr | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing |
title_full_unstemmed | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing |
title_short | A conserved dimer interface connects ERH and YTH family proteins to promote gene silencing |
title_sort | conserved dimer interface connects erh and yth family proteins to promote gene silencing |
url | https://doi.org/10.1038/s41467-018-08273-9 |
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