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==Cryo-EM structure of the human nucleosome lacking N-terminal region of H2A, H2B, H3, and H4==
<StructureSection load='8jla' size='340' side='right'caption='[[8jla]], [[Resolution|resolution]] 3.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8jla]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=8JLA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8JLA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.44&#8491;</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=8jla FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8jla OCA], [https://pdbe.org/8jla PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8jla RCSB], [https://www.ebi.ac.uk/pdbsum/8jla PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8jla ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome transcription by RNA polymerase II (RNAPII) has not been clarified. In the present study, we reconstituted nucleosomes lacking the N-terminal tail of each histone, H2A, H2B, H3 or H4, and performed RNAPII transcription assays. We found that the N-terminal tail of H3, but not H2A, H2B and H4, functions in RNAPII pausing at the SHL(-5) position of the nucleosome. Consistently, the RNAPII transcription assay also revealed that the nucleosome containing N-terminally acetylated H3 drastically alleviates RNAPII pausing at the SHL(-5) position. In addition, the H3 acetylated nucleosome produced increased amounts of the run-off transcript. These results provide important evidence that the H3 N-terminal tail plays a role in RNAPII pausing at the SHL(-5) position of the nucleosome, and its acetylation directly alleviates this nucleosome barrier.

Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II.,Oishi T, Hatazawa S, Kujirai T, Kato J, Kobayashi Y, Ogasawara M, Akatsu M, Ehara H, Sekine SI, Hayashi G, Takizawa Y, Kurumizaka H Nucleic Acids Res. 2023 Oct 27;51(19):10364-10374. doi: 10.1093/nar/gkad754. PMID:37718728<ref>PMID:37718728</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8jla" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Akatsu M]]
[[Category: Hatazawa S]]
[[Category: Kato J]]
[[Category: Kobayashi Y]]
[[Category: Kujirai T]]
[[Category: Kurumizaka H]]
[[Category: Ogasawara M]]
[[Category: Oishi T]]
[[Category: Takizawa Y]]