2l9s

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Revision as of 20:10, 1 August 2018

Solution structure of Pf1 SID1-mSin3A PAH2 Complex

Structural highlights

2l9s is a 2 chain structure with sequence from Human and Lk3 transgenic mice. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1s5q, 1s5r
Gene:	KIAA1523, Pf1, PHF12 (HUMAN), Kiaa4126, Sin3a (LK3 transgenic mice)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [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.^[2] ^[3] ^[4]

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^[5]

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
↑ Rao G, Alland L, Guida P, Schreiber-Agus N, Chen K, Chin L, Rochelle JM, Seldin MF, Skoultchi AI, DePinho RA. Mouse Sin3A interacts with and can functionally substitute for the amino-terminal repression of the Myc antagonist Mxi1. Oncogene. 1996 Mar 7;12(5):1165-72. PMID:8649810
↑ Ayer DE, Lawrence QA, Eisenman RN. Mad-Max transcriptional repression is mediated by ternary complex formation with mammalian homologs of yeast repressor Sin3. Cell. 1995 Mar 10;80(5):767-76. PMID:7889570
↑ Grimes JA, Nielsen SJ, Battaglioli E, Miska EA, Speh JC, Berry DL, Atouf F, Holdener BC, Mandel G, Kouzarides T. The co-repressor mSin3A is a functional component of the REST-CoREST repressor complex. J Biol Chem. 2000 Mar 31;275(13):9461-7. PMID:10734093
↑ 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

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2l9s"

@@ Line 1: / Line 1: @@
 ==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=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1s5q|1s5q]], [[1s5r|1s5r]]</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'>[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]</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>
 == Function ==

2l9s

From Proteopedia

Revision as of 20:10, 1 August 2018

Solution structure of Pf1 SID1-mSin3A PAH2 Complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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