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| | ==Solution structure of Pf1 SID1-mSin3A PAH2 Complex== | | ==Solution structure of Pf1 SID1-mSin3A PAH2 Complex== |
| - | <StructureSection load='2l9s' size='340' side='right' caption='[[2l9s]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l9s' size='340' side='right'caption='[[2l9s]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l9s]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human] and [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9S OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L9S FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l9s]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L9S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L9S FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s5q|1s5q]], [[1s5r|1s5r]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIAA1523, Pf1, PHF12 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), Kiaa4126, Sin3a ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=2l9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9s OCA], [https://pdbe.org/2l9s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l9s RCSB], [https://www.ebi.ac.uk/pdbsum/2l9s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9s ProSAT]</span></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=2l9s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l9s OCA], [http://pdbe.org/2l9s PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l9s RCSB], [http://www.ebi.ac.uk/pdbsum/2l9s PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l9s ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PHF12_HUMAN PHF12_HUMAN]] Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA.<ref>PMID:11390640</ref> [[http://www.uniprot.org/uniprot/SIN3A_MOUSE SIN3A_MOUSE]] Acts as a transcriptional repressor. Corepressor for REST. Interacts with MXI1 to repress MYC responsive genes and antagonize MYC oncogenic activities. Also interacts with MXD1-MAX heterodimers to repress transcription by tethering SIN3A to DNA. Acts cooperatively with OGT to repress transcription in parallel with histone deacetylation.<ref>PMID:8649810</ref> <ref>PMID:7889570</ref> <ref>PMID:10734093</ref> | + | [https://www.uniprot.org/uniprot/PHF12_HUMAN PHF12_HUMAN] Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA.<ref>PMID:11390640</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Large Structures]] |
| - | [[Category: Kumar, G Senthil]] | + | [[Category: Mus musculus]] |
| - | [[Category: Radhakrishnan, I]] | + | [[Category: Radhakrishnan I]] |
| - | [[Category: Xie, T]] | + | [[Category: Senthil Kumar G]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Xie T]] |
| - | [[Category: Amphipathic helix motif]] | + | [[Category: Zhang Y]] |
| - | [[Category: Protein-peptide complex]]
| + | |
| - | [[Category: Transcription]]
| + | |
| Structural highlights
Function
PHF12_HUMAN Acts as a transcriptional repressor. Involved in recruitment of functional SIN3A complexes to DNA. Represses transcription at least in part through the activity of an associated histone deacetylase (HDAC). May also repress transcription in a SIN3A-independent manner through recruitment of functional AES complexes to DNA.[1]
Publication Abstract from PubMed
Histone deacetylation constitutes an important mechanism for silencing genes. The histone-deacetylase-associated mammalian Rpd3S/Sin3S corepressor complex plays key roles in repressing aberrant gene transcription from cryptic transcription initiation sites and in mitigating RNA polymerase II progression in intragenic regions of actively transcribed genes. The Sin3 corepressor functions as a molecular adaptor linking histone deacetylases on the one hand, with the chromatin targeting subunits Pf1 and MRG15 on the other. Pf1 also functions as an adaptor by interacting with MRG15 and engaging in multivalent interactions with Sin3 targeting among other domains the two N-terminal paired amphipathic helix (PAH) domains that serve as sites of interaction with sequence-specific DNA-binding transcription factors. Here, we structurally and functionally evaluate the interaction between the PAH2 domain of mSin3A and the Sin3 interaction domain 1 (SID1) motif of Pf1 and find the structural aspects to be reminiscent of the interaction between the Mad1/Mxd1 transcription factor and Sin3. Pf1 residues within a highly conserved sequence motif immediately C-terminal to SID1 appear not to be important for the interaction with Sin3 PAH2. Unexpectedly, the MRG15 subunit competes, rather than collaborates, with Sin3 for the Pf1 segment encompassing the two conserved motifs, implying competition between two subunits for another subunit of the same chromatin-modifying complex.
Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex.,Kumar GS, Xie T, Zhang Y, Radhakrishnan I J Mol Biol. 2011 May 20;408(5):987-1000. Epub 2011 Apr 1. PMID:21440557[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yochum GS, Ayer DE. Pf1, a novel PHD zinc finger protein that links the TLE corepressor to the mSin3A-histone deacetylase complex. Mol Cell Biol. 2001 Jul;21(13):4110-8. PMID:11390640 doi:http://dx.doi.org/10.1128/MCB.21.13.4110-4118.2001
- ↑ Kumar GS, Xie T, Zhang Y, Radhakrishnan I. Solution Structure of the mSin3A PAH2-Pf1 SID1 Complex: A Mad1/Mxd1-Like Interaction Disrupted by MRG15 in the Rpd3S/Sin3S Complex. J Mol Biol. 2011 May 20;408(5):987-1000. Epub 2011 Apr 1. PMID:21440557 doi:10.1016/j.jmb.2011.03.043
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