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| | ==Class 3 : translocated nucleosome== | | ==Class 3 : translocated nucleosome== |
| - | <StructureSection load='6fq8' size='340' side='right' caption='[[6fq8]], [[Resolution|resolution]] 4.80Å' scene=''> | + | <SX load='6fq8' size='340' side='right' viewer='molstar' caption='[[6fq8]], [[Resolution|resolution]] 4.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6fq8]] is a 10 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQ8 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6FQ8 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6fq8]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6FQ8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6FQ8 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=6fq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fq8 OCA], [http://pdbe.org/6fq8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6fq8 RCSB], [http://www.ebi.ac.uk/pdbsum/6fq8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6fq8 ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.8Å</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=6fq8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6fq8 OCA], [https://pdbe.org/6fq8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6fq8 RCSB], [https://www.ebi.ac.uk/pdbsum/6fq8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6fq8 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/H3C_XENLA H3C_XENLA]] 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. [[http://www.uniprot.org/uniprot/H4_XENLA H4_XENLA]] 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. | + | [https://www.uniprot.org/uniprot/H3C_XENLA H3C_XENLA] 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. |
| | <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 6fq8" style="background-color:#fffaf0;"></div> | | <div class="pdbe-citations 6fq8" style="background-color:#fffaf0;"></div> |
| | + | |
| | + | ==See Also== |
| | + | *[[Histone 3D structures|Histone 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| - | </StructureSection> | + | </SX> |
| - | [[Category: Bilokapic, S]] | + | [[Category: Large Structures]] |
| - | [[Category: Halic, M]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Chromatin remodeling]] | + | [[Category: Xenopus laevis]] |
| - | [[Category: Cryo em]] | + | [[Category: Bilokapic S]] |
| - | [[Category: Gene regulation]] | + | [[Category: Halic M]] |
| - | [[Category: Nucleosome]]
| + | |
| - | [[Category: Nucleosome sliding]]
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| Structural highlights
Function
H3C_XENLA 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.
Publication Abstract from PubMed
Nucleosomes, the basic unit of chromatin, package and regulate expression of eukaryotic genomes. Nucleosomes are highly dynamic and are remodeled with the help of ATP-dependent remodeling factors. Yet, the mechanism of DNA translocation around the histone octamer is poorly understood. In this study, we present several nucleosome structures showing histone proteins and DNA in different organizational states. We observe that the histone octamer undergoes conformational changes that distort the overall nucleosome structure. As such, rearrangements in the histone core alpha-helices and DNA induce strain that distorts and moves DNA at SHL 2. Distortion of the nucleosome structure detaches histone alpha-helices from the DNA, leading to their rearrangement and DNA translocation. Biochemical assays show that cross-linked histone octamers are immobilized on DNA, indicating that structural changes in the octamer move DNA. This intrinsic plasticity of the nucleosome is exploited by chromatin remodelers and might be used by other chromatin machineries.
Structural rearrangements of the histone octamer translocate DNA.,Bilokapic S, Strauss M, Halic M Nat Commun. 2018 Apr 6;9(1):1330. doi: 10.1038/s41467-018-03677-z. PMID:29626188[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Bilokapic S, Strauss M, Halic M. Structural rearrangements of the histone octamer translocate DNA. Nat Commun. 2018 Apr 6;9(1):1330. doi: 10.1038/s41467-018-03677-z. PMID:29626188 doi:http://dx.doi.org/10.1038/s41467-018-03677-z
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