9dch

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(New page: '''Unreleased structure''' The entry 9dch is ON HOLD Authors: Song, J.S., Kasinath, V.K. Description: Single-stranded RNA-mediated PRC2 dimer Category: Unreleased Structures [[Cate...)
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'''Unreleased structure'''
 
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The entry 9dch is ON HOLD
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==Single-stranded RNA-mediated PRC2 dimer==
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<StructureSection load='9dch' size='340' side='right'caption='[[9dch]], [[Resolution|resolution]] 3.40&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9dch]] is a 13 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9DCH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9DCH FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.4&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9dch FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9dch OCA], [https://pdbe.org/9dch PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9dch RCSB], [https://www.ebi.ac.uk/pdbsum/9dch PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9dch ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN] Weaver syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/EZH2_HUMAN EZH2_HUMAN] Polycomb group (PcG) protein. Catalytic subunit of the PRC2/EED-EZH2 complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. Able to mono-, di- and trimethylate 'Lys-27' of histone H3 to form H3K27me1, H3K27me2 and H3K27me3, respectively. Compared to EZH2-containing complexes, it is more abundant in embryonic stem cells and plays a major role in forming H3K27me3, which is required for embryonic stem cell identity and proper differentiation. The PRC2/EED-EZH2 complex may also serve as a recruiting platform for DNA methyltransferases, thereby linking two epigenetic repression systems. Genes repressed by the PRC2/EED-EZH2 complex include HOXC8, HOXA9, MYT1, CDKN2A and retinoic acid target genes. EZH2 can also methylate non-histone proteins such as the transcription factor GATA4 and the nuclear receptor RORA.<ref>PMID:14532106</ref> <ref>PMID:15385962</ref> <ref>PMID:15231737</ref> <ref>PMID:15225548</ref> <ref>PMID:16179254</ref> <ref>PMID:16618801</ref> <ref>PMID:16357870</ref> <ref>PMID:16936726</ref> <ref>PMID:17210787</ref> <ref>PMID:17344414</ref> <ref>PMID:19026781</ref> <ref>PMID:18285464</ref> <ref>PMID:20935635</ref> <ref>PMID:23063525</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Methyltransferase PRC2 (Polycomb Repressive Complex 2) introduces histone H3K27 trimethylation, a repressive chromatin mark, to tune the differential expression of genes. PRC2 is precisely regulated by accessory proteins, histone post-translational modifications and, notably, RNA. Research on PRC2-associated RNA has mostly focused on the tight-binding G-quadruplex (G4) RNAs, which inhibit PRC2 enzymatic activity in vitro and in cells. Our recent cryo-EM structure provided a molecular mechanism for G4 RNA inactivating PRC2 via dimerization, but it remained unclear how diverse RNAs associate with and regulate PRC2. Here, we show that a single-stranded G-rich RNA and an atypical G4 structure called pUG-fold unexpectedly also mediate near-identical PRC2 dimerization resulting in inhibition of PRC2 methyltransferase activity. The conformational flexibility of arginine-rich loops within subunits EZH2 and AEBP2 of PRC2 can accommodate diverse RNA secondary structures, resulting in protein-RNA and protein-protein interfaces similar to those observed previously with G4 RNA. Furthermore, we address a recent report that failed to detect PRC2-associated RNAs in living cells by demonstrating the insensitivity of PRC2-RNA interaction to photochemical crosslinking. Our results support the significance of RNA-mediated PRC2 regulation by showing that this interaction is not limited to a single RNA secondary structure, consistent with the broad PRC2 transcriptome containing many G-tract RNAs incapable of folding into G4 structures.
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Authors: Song, J.S., Kasinath, V.K.
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Diverse RNA Structures Induce PRC2 Dimerization and Inhibit Histone Methyltransferase Activity.,Song J, Yao L, Gooding AR, Thron V, Kasinath V, Cech TR bioRxiv [Preprint]. 2024 Aug 29:2024.08.29.610323. doi: , 10.1101/2024.08.29.610323. PMID:39257770<ref>PMID:39257770</ref>
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Description: Single-stranded RNA-mediated PRC2 dimer
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: Kasinath, V.K]]
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<div class="pdbe-citations 9dch" style="background-color:#fffaf0;"></div>
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[[Category: Song, J.S]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Kasinath VK]]
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[[Category: Song JS]]

Current revision

Single-stranded RNA-mediated PRC2 dimer

PDB ID 9dch

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