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| | ==Crystal Structure of the heterotypic nucleosome containing human CENP-A and H3.3== | | ==Crystal Structure of the heterotypic nucleosome containing human CENP-A and H3.3== |
| - | <StructureSection load='3wtp' size='340' side='right' caption='[[3wtp]], [[Resolution|resolution]] 2.67Å' scene=''> | + | <StructureSection load='3wtp' size='340' side='right'caption='[[3wtp]], [[Resolution|resolution]] 2.67Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3wtp]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WTP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3WTP FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3wtp]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3WTP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3WTP FirstGlance]. <br> |
| - | </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=3wtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wtp OCA], [http://pdbe.org/3wtp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3wtp RCSB], [http://www.ebi.ac.uk/pdbsum/3wtp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3wtp ProSAT]</span></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]] 2.67Å</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=3wtp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3wtp OCA], [https://pdbe.org/3wtp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3wtp RCSB], [https://www.ebi.ac.uk/pdbsum/3wtp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3wtp ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/H2B1J_HUMAN H2B1J_HUMAN]] Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid.<ref>PMID:11859126</ref> <ref>PMID:12860195</ref> <ref>PMID:15019208</ref> [[http://www.uniprot.org/uniprot/CENPA_HUMAN CENPA_HUMAN]] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).<ref>PMID:20739937</ref> <ref>PMID:21478274</ref> | + | [https://www.uniprot.org/uniprot/CENPA_HUMAN CENPA_HUMAN] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).<ref>PMID:20739937</ref> <ref>PMID:21478274</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: Almouzni, G]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Arimura, Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Fujita, R]] | + | [[Category: Almouzni G]] |
| - | [[Category: Fukagawa, T]] | + | [[Category: Arimura Y]] |
| - | [[Category: Horikoshi, N]] | + | [[Category: Fujita R]] |
| - | [[Category: Kagawa, W]] | + | [[Category: Fukagawa T]] |
| - | [[Category: Kurumizaka, H]] | + | [[Category: Horikoshi N]] |
| - | [[Category: Shirayama, K]] | + | [[Category: Kagawa W]] |
| - | [[Category: Chromatin formation]]
| + | [[Category: Kurumizaka H]] |
| - | [[Category: Dna binding]]
| + | [[Category: Shirayama K]] |
| - | [[Category: Dna binding protein-dna complex]]
| + | |
| - | [[Category: Histone fold]]
| + | |
| Structural highlights
Function
CENPA_HUMAN Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore. Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation. May serve as an epigenetic mark that propagates centromere identity through replication and cell division. The CENPA-H4 heterotetramer can bind DNA by itself (in vitro).[1] [2]
Publication Abstract from PubMed
The centromere-specific histone H3 variant, CENP-A, is overexpressed in particular aggressive cancer cells, where it can be mislocalized ectopically in the form of heterotypic nucleosomes containing H3.3. In the present study, we report the crystal structure of the heterotypic CENP-A/H3.3 particle and reveal its "hybrid structure", in which the physical characteristics of CENP-A and H3.3 are conserved independently within the same particle. The CENP-A/H3.3 nucleosome forms an unexpectedly stable structure as compared to the CENP-A nucleosome, and allows the binding of the essential centromeric protein, CENP-C, which is ectopically mislocalized in the chromosomes of CENP-A overexpressing cells.
Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3.,Arimura Y, Shirayama K, Horikoshi N, Fujita R, Taguchi H, Kagawa W, Fukagawa T, Almouzni G, Kurumizaka H Sci Rep. 2014 Nov 19;4:7115. doi: 10.1038/srep07115. PMID:25408271[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sekulic N, Bassett EA, Rogers DJ, Black BE. The structure of (CENP-A-H4)(2) reveals physical features that mark centromeres. Nature. 2010 Aug 25. PMID:20739937 doi:10.1038/nature09323
- ↑ Hu H, Liu Y, Wang M, Fang J, Huang H, Yang N, Li Y, Wang J, Yao X, Shi Y, Li G, Xu RM. Structure of a CENP-A-histone H4 heterodimer in complex with chaperone HJURP. Genes Dev. 2011 May 1;25(9):901-6. Epub 2011 Apr 8. PMID:21478274 doi:10.1101/gad.2045111
- ↑ Arimura Y, Shirayama K, Horikoshi N, Fujita R, Taguchi H, Kagawa W, Fukagawa T, Almouzni G, Kurumizaka H. Crystal structure and stable property of the cancer-associated heterotypic nucleosome containing CENP-A and H3.3. Sci Rep. 2014 Nov 19;4:7115. doi: 10.1038/srep07115. PMID:25408271 doi:http://dx.doi.org/10.1038/srep07115
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