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| <StructureSection load='5j8y' size='340' side='right'caption='[[5j8y]], [[Resolution|resolution]] 1.98Å' scene=''> | | <StructureSection load='5j8y' size='340' side='right'caption='[[5j8y]], [[Resolution|resolution]] 1.98Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[5j8y]] is a 4 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=5J8Y OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5J8Y FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5j8y]] is a 4 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=5J8Y OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5J8Y FirstGlance]. <br> |
- | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Scm, CG9495 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME]), Sfmbt, CG16975 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=7227 DROME])</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]] 1.98Å</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5j8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8y OCA], [http://pdbe.org/5j8y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5j8y RCSB], [http://www.ebi.ac.uk/pdbsum/5j8y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8y 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=5j8y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5j8y OCA], [https://pdbe.org/5j8y PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5j8y RCSB], [https://www.ebi.ac.uk/pdbsum/5j8y PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5j8y ProSAT]</span></td></tr> |
| </table> | | </table> |
| == Function == | | == Function == |
- | [[http://www.uniprot.org/uniprot/SCM_DROME SCM_DROME]] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.<ref>PMID:15280237</ref> [UniProtKB:Q9W3C1] [[http://www.uniprot.org/uniprot/SMBT_DROME SMBT_DROME]] Polycomb group (PcG) protein that binds to the Polycomb response elements (PREs) found in the regulatory regions of many genes. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility. Necessary but not sufficient to recruit a functional PcG repressive complex that represses target genes, suggesting that the recruitment of the distinct PRC1 complex is also required to allow a subsequent repression.<ref>PMID:16618800</ref> | + | [https://www.uniprot.org/uniprot/SCM_DROME SCM_DROME] Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.<ref>PMID:15280237</ref> [UniProtKB:Q9W3C1] |
| <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: Benda, C]] | + | [[Category: Benda C]] |
- | [[Category: Frey, F]] | + | [[Category: Frey F]] |
- | [[Category: Mueller, J]] | + | [[Category: Mueller J]] |
- | [[Category: Drosophila]]
| + | |
- | [[Category: Nuclear protein]]
| + | |
- | [[Category: Prc1 phorc sam domain polycom response element]]
| + | |
- | [[Category: Signaling protein]]
| + | |
| Structural highlights
Function
SCM_DROME Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via the methylation of histones, rendering chromatin heritably changed in its expressibility.[1] [UniProtKB:Q9W3C1]
Publication Abstract from PubMed
Polycomb group (PcG) protein complexes repress transcription by modifying target gene chromatin. In Drosophila, this repression requires association of PcG protein complexes with cis-regulatory Polycomb response elements (PREs), but the interactions permitting formation of these assemblies are poorly understood. We show that the Sfmbt subunit of the DNA-binding Pho-repressive complex (PhoRC) and the Scm subunit of the canonical Polycomb-repressive complex 1 (PRC1) directly bind each other through their SAM domains. The 1.9 A crystal structure of the Scm-SAM:Sfmbt-SAM complex reveals the recognition mechanism and shows that Sfmbt-SAM lacks the polymerization capacity of the SAM domains of Scm and its PRC1 partner subunit, Ph. Functional analyses in Drosophila demonstrate that Sfmbt-SAM and Scm-SAM are essential for repression and that PhoRC DNA binding is critical to initiate PRC1 association with PREs. Together, this suggests that PRE-tethered Sfmbt-SAM nucleates PRC1 recruitment and that Scm-SAM/Ph-SAM-mediated polymerization then results in the formation of PRC1-compacted chromatin.
Molecular basis of PRC1 targeting to Polycomb response elements by PhoRC.,Frey F, Sheahan T, Finkl K, Stoehr G, Mann M, Benda C, Muller J Genes Dev. 2016 May 1;30(9):1116-27. doi: 10.1101/gad.279141.116. PMID:27151979[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Peterson AJ, Mallin DR, Francis NJ, Ketel CS, Stamm J, Voeller RK, Kingston RE, Simon JA. Requirement for sex comb on midleg protein interactions in Drosophila polycomb group repression. Genetics. 2004 Jul;167(3):1225-39. PMID:15280237 doi:http://dx.doi.org/10.1534/genetics.104.027474
- ↑ Frey F, Sheahan T, Finkl K, Stoehr G, Mann M, Benda C, Muller J. Molecular basis of PRC1 targeting to Polycomb response elements by PhoRC. Genes Dev. 2016 May 1;30(9):1116-27. doi: 10.1101/gad.279141.116. PMID:27151979 doi:http://dx.doi.org/10.1101/gad.279141.116
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