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| | <StructureSection load='2yb8' size='340' side='right'caption='[[2yb8]], [[Resolution|resolution]] 2.30Å' scene=''> | | <StructureSection load='2yb8' size='340' side='right'caption='[[2yb8]], [[Resolution|resolution]] 2.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2yb8]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Drome Drome]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YB8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2YB8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2yb8]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2YB8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YB8 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.3Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2xyi|2xyi]], [[2yba|2yba]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2yb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb8 OCA], [http://pdbe.org/2yb8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2yb8 RCSB], [http://www.ebi.ac.uk/pdbsum/2yb8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2yb8 ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yb8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yb8 OCA], [https://pdbe.org/2yb8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yb8 RCSB], [https://www.ebi.ac.uk/pdbsum/2yb8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yb8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/SUZ12_DROME SUZ12_DROME]] Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required. [[http://www.uniprot.org/uniprot/CAF1_DROME CAF1_DROME]] Core histone-binding subunit that may target chromatin assembly factors, chromatin remodeling factors and histone deacetylases to their histone substrates in a manner that is regulated by nucleosomal DNA. Component of several complexes which regulate chromatin metabolism. These include the chromatin assembly factor 1 (CAF-1) complex, which is required for chromatin assembly following DNA replication and DNA repair; the nucleosome remodeling and deacetylase complex (the NuRD complex), which promotes transcriptional repression by histone deacetylation and nucleosome remodeling; the nucleosome remodeling factor (NURF) complex, which catalyzes ATP-dependent nucleosome sliding and facilitates transcription of chromatin; and the polycomb group (PcG) repressor complex ESC-E(Z), which promotes repression of homeotic genes during development. Also required for transcriptional repression of E2F target genes by E2f2 and Rbf or Rbf2.<ref>PMID:8887645</ref> <ref>PMID:9419341</ref> <ref>PMID:9784495</ref> <ref>PMID:12490953</ref> <ref>PMID:15456884</ref> | + | [https://www.uniprot.org/uniprot/SUZ12_DROME SUZ12_DROME] Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| - | *[[Polycomb|Polycomb]] | + | *[[Polycomb complex proteins 3D structures|Polycomb complex proteins 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Drome]] | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Aiwazian, J]] | + | [[Category: Aiwazian J]] |
| - | [[Category: Bauer, A]] | + | [[Category: Bauer A]] |
| - | [[Category: Bouwmeester, T]] | + | [[Category: Bouwmeester T]] |
| - | [[Category: Bunker, R D]] | + | [[Category: Bunker RD]] |
| - | [[Category: Chan, H]] | + | [[Category: Chan H]] |
| - | [[Category: Faty, M]] | + | [[Category: Faty M]] |
| - | [[Category: Fischle, W]] | + | [[Category: Fischle W]] |
| - | [[Category: Gu, J]] | + | [[Category: Gu J]] |
| - | [[Category: Gut, H]] | + | [[Category: Gut H]] |
| - | [[Category: Hess, D]] | + | [[Category: Hess D]] |
| - | [[Category: Li, L]] | + | [[Category: Li L]] |
| - | [[Category: Lingaraju, G M]] | + | [[Category: Lingaraju GM]] |
| - | [[Category: Ly-Hartig, N]] | + | [[Category: Ly-Hartig N]] |
| - | [[Category: Muller, J]] | + | [[Category: Muller J]] |
| - | [[Category: Prusty, A B]] | + | [[Category: Prusty AB]] |
| - | [[Category: Sack, R]] | + | [[Category: Sack R]] |
| - | [[Category: Schmitges, F W]] | + | [[Category: Schmitges FW]] |
| - | [[Category: Stutzer, A]] | + | [[Category: Stutzer A]] |
| - | [[Category: Thoma, N H]] | + | [[Category: Thoma NH]] |
| - | [[Category: Wirth, U]] | + | [[Category: Wirth U]] |
| - | [[Category: Zhao, K]] | + | [[Category: Zhao K]] |
| - | [[Category: Zhou, S]] | + | [[Category: Zhou S]] |
| - | [[Category: Chromatin remodelling]]
| + | |
| - | [[Category: H3k27]]
| + | |
| - | [[Category: H3k4]]
| + | |
| - | [[Category: H4]]
| + | |
| - | [[Category: Histone methlyation]]
| + | |
| - | [[Category: P55]]
| + | |
| - | [[Category: Prc2]]
| + | |
| - | [[Category: Rbap46]]
| + | |
| - | [[Category: Rbap48]]
| + | |
| - | [[Category: Rbbp4]]
| + | |
| - | [[Category: Rbbp7]]
| + | |
| - | [[Category: Transcription]]
| + | |
| - | [[Category: Wd40 domain]]
| + | |
| Structural highlights
Function
SUZ12_DROME Polycomb group (PcG) protein. While PcG proteins are generally required to maintain the transcriptionally repressive state of homeotic genes throughout development, this protein is specifically required during the first 6 hours of embryogenesis to establish the repressed state. Component of the Esc/E(z) complex, which methylates 'Lys-9' (H3K9me) and 'Lys-27' (H3K27me) of histone H3, leading to transcriptional repression of the affected target gene. The Esc/E(z) complex is necessary but not sufficient for the repression of homeotic target genes, suggesting that the recruitment of the distinct PRC1 complex is also required.
Publication Abstract from PubMed
The Polycomb repressive complex 2 (PRC2) confers transcriptional repression through histone H3 lysine 27 trimethylation (H3K27me3). Here, we examined how PRC2 is modulated by histone modifications associated with transcriptionally active chromatin. We provide the molecular basis of histone H3 N terminus recognition by the PRC2 Nurf55-Su(z)12 submodule. Binding of H3 is lost if lysine 4 in H3 is trimethylated. We find that H3K4me3 inhibits PRC2 activity in an allosteric fashion assisted by the Su(z)12 C terminus. In addition to H3K4me3, PRC2 is inhibited by H3K36me2/3 (i.e., both H3K36me2 and H3K36me3). Direct PRC2 inhibition by H3K4me3 and H3K36me2/3 active marks is conserved in humans, mouse, and fly, rendering transcriptionally active chromatin refractory to PRC2 H3K27 trimethylation. While inhibition is present in plant PRC2, it can be modulated through exchange of the Su(z)12 subunit. Inhibition by active chromatin marks, coupled to stimulation by transcriptionally repressive H3K27me3, enables PRC2 to autonomously template repressive H3K27me3 without overwriting active chromatin domains.
Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks.,Schmitges FW, Prusty AB, Faty M, Stutzer A, Lingaraju GM, Aiwazian J, Sack R, Hess D, Li L, Zhou S, Bunker RD, Wirth U, Bouwmeester T, Bauer A, Ly-Hartig N, Zhao K, Chan H, Gu J, Gut H, Fischle W, Muller J, Thoma NH Mol Cell. 2011 May 6;42(3):330-41. PMID:21549310[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Schmitges FW, Prusty AB, Faty M, Stutzer A, Lingaraju GM, Aiwazian J, Sack R, Hess D, Li L, Zhou S, Bunker RD, Wirth U, Bouwmeester T, Bauer A, Ly-Hartig N, Zhao K, Chan H, Gu J, Gut H, Fischle W, Muller J, Thoma NH. Histone Methylation by PRC2 Is Inhibited by Active Chromatin Marks. Mol Cell. 2011 May 6;42(3):330-41. PMID:21549310 doi:10.1016/j.molcel.2011.03.025
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