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| | ==The structure of the carboxy-terminal domain of DNTTIP1== | | ==The structure of the carboxy-terminal domain of DNTTIP1== |
| - | <StructureSection load='2mwi' size='340' side='right'caption='[[2mwi]], [[NMR_Ensembles_of_Models | 65 NMR models]]' scene=''> | + | <StructureSection load='2mwi' size='340' side='right'caption='[[2mwi]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2mwi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MWI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2mwi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MWI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MWI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">DNTTIP1, C20orf167, TDIF1 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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=2mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwi OCA], [https://pdbe.org/2mwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwi RCSB], [https://www.ebi.ac.uk/pdbsum/2mwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwi 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=2mwi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mwi OCA], [https://pdbe.org/2mwi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mwi RCSB], [https://www.ebi.ac.uk/pdbsum/2mwi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mwi ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TDIF1_HUMAN TDIF1_HUMAN]] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.<ref>PMID:11473582</ref> <ref>PMID:23874396</ref>
| + | [https://www.uniprot.org/uniprot/TDIF1_HUMAN TDIF1_HUMAN] Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.<ref>PMID:11473582</ref> <ref>PMID:23874396</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: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Itoh, T]] | + | [[Category: Itoh T]] |
| - | [[Category: Muskett, F W]] | + | [[Category: Muskett FW]] |
| - | [[Category: Schwabe, J W.R]] | + | [[Category: Schwabe JWR]] |
| - | [[Category: Dnttip1]]
| + | |
| - | [[Category: Gene expression]]
| + | |
| - | [[Category: Hdac]]
| + | |
| - | [[Category: Hdac1]]
| + | |
| - | [[Category: Histone deacetylase]]
| + | |
| - | [[Category: Midea]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Tdif1]]
| + | |
| Structural highlights
Function
TDIF1_HUMAN Shown to enhance TdT activity, in vitro. Also acts as a transcriptional regulator, binding to the consensus sequence 5'-GNTGCATG-3' following an AT-tract. Associates with RAB20 promoter and positively regulates its transcription.[1] [2]
Publication Abstract from PubMed
Recent proteomic studies have identified a novel histone deacetylase complex that is upregulated during mitosis and is associated with cyclin A. This complex is conserved from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly understood. Here, we report the structures of two domains from DNTTIP1. The amino-terminal region forms a tight dimerization domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxy-terminal domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain, despite lacking obvious sequence homology. We show that this domain in DNTTIP1 mediates interaction with both DNA and nucleosomes. Thus, DNTTIP1 acts as a dimeric chromatin binding module in the HDAC1:MIDEAS corepressor complex.
Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.,Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yamashita N, Shimazaki N, Ibe S, Kaneko R, Tanabe A, Toyomoto T, Fujita K, Hasegawa T, Toji S, Tamai K, Yamamoto H, Koiwai O. Terminal deoxynucleotidyltransferase directly interacts with a novel nuclear protein that is homologous to p65. Genes Cells. 2001 Jul;6(7):641-52. PMID:11473582
- ↑ Kubota T, Koiwai O, Hori K, Watanabe N, Koiwai K. TdIF1 recognizes a specific DNA sequence through its Helix-Turn-Helix and AT-hook motifs to regulate gene transcription. PLoS One. 2013 Jul 10;8(7):e66710. doi: 10.1371/journal.pone.0066710. Print 2013. PMID:23874396 doi:http://dx.doi.org/10.1371/journal.pone.0066710
- ↑ Itoh T, Fairall L, Muskett FW, Milano CP, Watson PJ, Arnaudo N, Saleh A, Millard CJ, El-Mezgueldi M, Martino F, Schwabe JW. Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. Nucleic Acids Res. 2015 Feb 4. pii: gkv068. PMID:25653165 doi:http://dx.doi.org/10.1093/nar/gkv068
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