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 and Chengmin Qian ()
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Yongming Du: The University of Hong Kong
Yinxia Yan: The University of Hong Kong
Si Xie: The University of Hong Kong
Hao Huang: The City University of Hong Kong
Xin Wang: The City University of Hong Kong
Ray Kit Ng: The University of Hong Kong
Ming-Ming Zhou: Icahn School of Medicine at Mount Sinai
Chengmin Qian: The University of Hong Kong

Nature Communications, 2021, vol. 12, issue 1, 1-9

Abstract: Abstract Spindlin1 is a unique multivalent epigenetic reader that facilitates ribosomal RNA transcription. In this study, we provide molecular and structural basis by which Spindlin1 acts in complex with C11orf84 to preferentially recognize non-canonical bivalent mark of trimethylated lysine 4 and lysine 9 present on the same histone H3 tail (H3K4me3K9me3). We demonstrate that C11orf84 binding stabilizes Spindlin1 and enhances its association with bivalent H3K4me3K9me3 mark. The functional analysis suggests that Spindlin1/C11orf84 complex can displace HP1 proteins from H3K4me3K9me3-enriched rDNA loci, thereby facilitating the conversion of these poised rDNA repeats from the repressed state to the active conformation, and the consequent recruitment of RNA Polymerase I for rRNA transcription. Our study uncovers a previously unappreciated mechanism of bivalent H3K4me3K9me3 recognition by Spindlin1/C11orf84 complex required for activation of rRNA transcription.

Date: 2021
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DOI: 10.1038/s41467-021-21236-x

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