Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation

Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation

Spindlin1 is an epigenetic reader that facilitates ribosomal RNA transcription. Here the authors reveal in vitro and structural evidence suggesting that Spindlin1 acts together with C11orf84 to recognize noncanonical bivalent mark of trimethylated lysine 4 and lysine 9 present on histone H3 tail (H3...

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Autores principales: Yongming Du, Yinxia Yan, Si Xie, Hao Huang, Xin Wang, Ray Kit Ng, Ming-Ming Zhou, Chengmin Qian
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2021
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Acceso en línea:https://doaj.org/article/8b9fb4e872854524b654cba256ef7a51
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spelling oai:doaj.org-article:8b9fb4e872854524b654cba256ef7a512021-12-02T12:14:48ZStructural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation10.1038/s41467-021-21236-x2041-1723https://doaj.org/article/8b9fb4e872854524b654cba256ef7a512021-02-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-21236-xhttps://doaj.org/toc/2041-1723Spindlin1 is an epigenetic reader that facilitates ribosomal RNA transcription. Here the authors reveal in vitro and structural evidence suggesting that Spindlin1 acts together with C11orf84 to recognize noncanonical bivalent mark of trimethylated lysine 4 and lysine 9 present on histone H3 tail (H3K4me3K9me3).Yongming DuYinxia YanSi XieHao HuangXin WangRay Kit NgMing-Ming ZhouChengmin QianNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Yongming Du
Yinxia Yan
Si Xie
Hao Huang
Xin Wang
Ray Kit Ng
Ming-Ming Zhou
Chengmin Qian
Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
description Spindlin1 is an epigenetic reader that facilitates ribosomal RNA transcription. Here the authors reveal in vitro and structural evidence suggesting that Spindlin1 acts together with C11orf84 to recognize noncanonical bivalent mark of trimethylated lysine 4 and lysine 9 present on histone H3 tail (H3K4me3K9me3).
format article
author Yongming Du
Yinxia Yan
Si Xie
Hao Huang
Xin Wang
Ray Kit Ng
Ming-Ming Zhou
Chengmin Qian
author_facet Yongming Du
Yinxia Yan
Si Xie
Hao Huang
Xin Wang
Ray Kit Ng
Ming-Ming Zhou
Chengmin Qian
author_sort Yongming Du
title Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
title_short Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
title_full Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
title_fullStr Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
title_full_unstemmed Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
title_sort structural mechanism of bivalent histone h3k4me3k9me3 recognition by the spindlin1/c11orf84 complex in rrna transcription activation
publisher Nature Portfolio
publishDate 2021
url https://doaj.org/article/8b9fb4e872854524b654cba256ef7a51
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