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

Yongming Du; Yinxia Yan; Si Xie; Hao Huang; Xin Wang; Ray Kit Ng; Ming-Ming Zhou; Chengmin Qian

doi:10.1038/s41467-021-21236-x

Nature Communications (Feb 2021)

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

Yongming Du,
Yinxia Yan,
Si Xie,
Hao Huang,
Xin Wang,
Ray Kit Ng,
Ming-Ming Zhou,
Chengmin Qian

Affiliations

Yongming Du: School of Biomedical Sciences, The University of Hong Kong
Yinxia Yan: School of Biomedical Sciences, The University of Hong Kong
Si Xie: School of Biomedical Sciences, The University of Hong Kong
Hao Huang: Department of Biomedical Sciences, The City University of Hong Kong
Xin Wang: Department of Biomedical Sciences, The City University of Hong Kong
Ray Kit Ng: School of Biomedical Sciences, The University of Hong Kong
Ming-Ming Zhou: Department of Pharmacological Sciences, Icahn School of Medicine at Mount Sinai
Chengmin Qian: School of Biomedical Sciences, The University of Hong Kong

DOI: https://doi.org/10.1038/s41467-021-21236-x
Journal volume & issue: Vol. 12, no. 1
pp. 1 – 9

Abstract

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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).

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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