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| | <StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47Å' scene=''> | | <StructureSection load='6xwt' size='340' side='right'caption='[[6xwt]], [[Resolution|resolution]] 3.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6xwt]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6XWT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6XWT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6xwt]] is a 6 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=6XWT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6XWT 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=6xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwt OCA], [http://pdbe.org/6xwt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6xwt RCSB], [http://www.ebi.ac.uk/pdbsum/6xwt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwt 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]] 3.47Å</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=6xwt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6xwt OCA], [https://pdbe.org/6xwt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6xwt RCSB], [https://www.ebi.ac.uk/pdbsum/6xwt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6xwt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CID_DROME CID_DROME]] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore (PubMed:11483958, PubMed:16839185). Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation (PubMed:24703848, PubMed:11483958, PubMed:16839185). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:11483958, PubMed:16839185).<ref>PMID:11483958</ref> <ref>PMID:16839185</ref> <ref>PMID:24703848</ref> [[http://www.uniprot.org/uniprot/A0A0B4KFZ9_DROME A0A0B4KFZ9_DROME]] 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.[RuleBase:RU000528][SAAS:SAAS00581158] | + | [https://www.uniprot.org/uniprot/CID_DROME CID_DROME] Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore (PubMed:11483958, PubMed:16839185). Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation (PubMed:24703848, PubMed:11483958, PubMed:16839185). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:11483958, PubMed:16839185).<ref>PMID:11483958</ref> <ref>PMID:16839185</ref> <ref>PMID:24703848</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </div> | | </div> |
| | <div class="pdbe-citations 6xwt" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6xwt" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone 3D structures|Histone 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Drosophila melanogaster]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Abad, M A]] | + | [[Category: Abad MA]] |
| - | [[Category: Byron, O]] | + | [[Category: Byron O]] |
| - | [[Category: Heun, P]] | + | [[Category: Heun P]] |
| - | [[Category: Jeyaprakash, A A]] | + | [[Category: Jeyaprakash AA]] |
| - | [[Category: Lazou, V]] | + | [[Category: Lazou V]] |
| - | [[Category: Medina-Pritchard, B]] | + | [[Category: Medina-Pritchard B]] |
| - | [[Category: Rappsilber, J]] | + | [[Category: Rappsilber J]] |
| - | [[Category: Zou, J]] | + | [[Category: Zou J]] |
| - | [[Category: Cell cycle]]
| + | |
| - | [[Category: Cell division]]
| + | |
| - | [[Category: Centromere]]
| + | |
| - | [[Category: Kinetochore]]
| + | |
| Structural highlights
Function
CID_DROME Histone H3-like variant which exclusively replaces conventional H3 in the nucleosome core of centromeric chromatin at the inner plate of the kinetochore (PubMed:11483958, PubMed:16839185). Required for recruitment and assembly of kinetochore proteins, mitotic progression and chromosome segregation (PubMed:24703848, PubMed:11483958, PubMed:16839185). May serve as an epigenetic mark that propagates centromere identity through replication and cell division (PubMed:11483958, PubMed:16839185).[1] [2] [3]
Publication Abstract from PubMed
Centromeres are microtubule attachment sites on chromosomes defined by the enrichment of histone variant CENP-A-containing nucleosomes. To preserve centromere identity, CENP-A must be escorted to centromeres by a CENP-A-specific chaperone for deposition. Despite this essential requirement, many eukaryotes differ in the composition of players involved in centromere maintenance, highlighting the plasticity of this process. In humans, CENP-A recognition and centromere targeting are achieved by HJURP and the Mis18 complex, respectively. Using X-ray crystallography, we here show how Drosophila CAL1, an evolutionarily distinct CENP-A histone chaperone, binds both CENP-A and the centromere receptor CENP-C without the requirement for the Mis18 complex. While an N-terminal CAL1 fragment wraps around CENP-A/H4 through multiple physical contacts, a C-terminal CAL1 fragment directly binds a CENP-C cupin domain dimer. Although divergent at the primary structure level, CAL1 thus binds CENP-A/H4 using evolutionarily conserved and adaptive structural principles. The CAL1 binding site on CENP-C is strategically positioned near the cupin dimerisation interface, restricting binding to just one CAL1 molecule per CENP-C dimer. Overall, by demonstrating how CAL1 binds CENP-A/H4 and CENP-C, we provide key insights into the minimalistic principles underlying centromere maintenance.
Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1.,Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA EMBO J. 2020 Mar 5:e103234. doi: 10.15252/embj.2019103234. PMID:32134144[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Blower MD, Karpen GH. The role of Drosophila CID in kinetochore formation, cell-cycle progression and heterochromatin interactions. Nat Cell Biol. 2001 Aug;3(8):730-9. doi: 10.1038/35087045. PMID:11483958 doi:http://dx.doi.org/10.1038/35087045
- ↑ Blower MD, Daigle T, Kaufman T, Karpen GH. Drosophila CENP-A mutations cause a BubR1-dependent early mitotic delay without normal localization of kinetochore components. PLoS Genet. 2006 Jul;2(7):e110. Epub 2006 Jun 5. PMID:16839185 doi:http://dx.doi.org/05-PLGE-RA-0358R2
- ↑ Mathew V, Pauleau AL, Steffen N, Bergner A, Becker PB, Erhardt S. The histone-fold protein CHRAC14 influences chromatin composition in response to DNA damage. Cell Rep. 2014 Apr 24;7(2):321-330. doi: 10.1016/j.celrep.2014.03.008. Epub 2014 , Apr 3. PMID:24703848 doi:http://dx.doi.org/10.1016/j.celrep.2014.03.008
- ↑ Medina-Pritchard B, Lazou V, Zou J, Byron O, Abad MA, Rappsilber J, Heun P, Jeyaprakash AA. Structural basis for centromere maintenance by Drosophila CENP-A chaperone CAL1. EMBO J. 2020 Mar 5:e103234. doi: 10.15252/embj.2019103234. PMID:32134144 doi:http://dx.doi.org/10.15252/embj.2019103234
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