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- Publisher Website: 10.1038/s41467-021-21236-x
- Scopus: eid_2-s2.0-85101093856
- PMID: 33574238
- WOS: WOS:000620142700011
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Article: Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation
Title | Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation |
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Authors | |
Issue Date | 2021 |
Publisher | Nature Research: Fully open access journals. The Journal's web site is located at http://www.nature.com/ncomms/index.html |
Citation | Nature Communications, 2021, v. 12 n. 1, p. article no. 949 How to Cite? |
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. |
Persistent Identifier | http://hdl.handle.net/10722/297146 |
ISSN | 2023 Impact Factor: 14.7 2023 SCImago Journal Rankings: 4.887 |
PubMed Central ID | |
ISI Accession Number ID |
DC Field | Value | Language |
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dc.contributor.author | DU, Y | - |
dc.contributor.author | Yan, Y | - |
dc.contributor.author | Xie, S | - |
dc.contributor.author | Huang, H | - |
dc.contributor.author | Wang, X | - |
dc.contributor.author | Ng, RK | - |
dc.contributor.author | Zhou, MM | - |
dc.contributor.author | Qian, C | - |
dc.date.accessioned | 2021-03-08T07:14:49Z | - |
dc.date.available | 2021-03-08T07:14:49Z | - |
dc.date.issued | 2021 | - |
dc.identifier.citation | Nature Communications, 2021, v. 12 n. 1, p. article no. 949 | - |
dc.identifier.issn | 2041-1723 | - |
dc.identifier.uri | http://hdl.handle.net/10722/297146 | - |
dc.description.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. | - |
dc.language | eng | - |
dc.publisher | Nature Research: Fully open access journals. The Journal's web site is located at http://www.nature.com/ncomms/index.html | - |
dc.relation.ispartof | Nature Communications | - |
dc.rights | Nature Communications. Copyright © Nature Research: Fully open access journals. | - |
dc.rights | This work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License. | - |
dc.title | Structural mechanism of bivalent histone H3K4me3K9me3 recognition by the Spindlin1/C11orf84 complex in rRNA transcription activation | - |
dc.type | Article | - |
dc.identifier.email | Xie, S: xiesi@hku.hk | - |
dc.identifier.email | Qian, C: cmqian@hku.hk | - |
dc.identifier.authority | Ng, RK=rp00273 | - |
dc.identifier.authority | Qian, C=rp01371 | - |
dc.description.nature | published_or_final_version | - |
dc.identifier.doi | 10.1038/s41467-021-21236-x | - |
dc.identifier.pmid | 33574238 | - |
dc.identifier.pmcid | PMC7878818 | - |
dc.identifier.scopus | eid_2-s2.0-85101093856 | - |
dc.identifier.hkuros | 321575 | - |
dc.identifier.volume | 12 | - |
dc.identifier.issue | 1 | - |
dc.identifier.spage | article no. 949 | - |
dc.identifier.epage | article no. 949 | - |
dc.identifier.isi | WOS:000620142700011 | - |
dc.publisher.place | United Kingdom | - |