7pf3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[7pf3]] is a 11 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=7PF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PF3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pf3]] is a 11 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=7PF3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PF3 FirstGlance]. <br> | ||
</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=7pf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pf3 OCA], [https://pdbe.org/7pf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pf3 RCSB], [https://www.ebi.ac.uk/pdbsum/7pf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pf3 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]] 4Å</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=7pf3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pf3 OCA], [https://pdbe.org/7pf3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pf3 RCSB], [https://www.ebi.ac.uk/pdbsum/7pf3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pf3 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions. | Throughout the genome, nucleosomes often form regular arrays that differ in nucleosome repeat length (NRL), occupancy of linker histone H1 and transcriptional activity. Here, we report cryo-EM structures of human H1-containing tetranucleosome arrays with four physiologically relevant NRLs. The structures show a zig-zag arrangement of nucleosomes, with nucleosomes 1 and 3 forming a stack. H1 binding to stacked nucleosomes depends on the NRL, whereas H1 always binds to the non-stacked nucleosomes 2 and 4. Short NRLs lead to altered trajectories of linker DNA, and these altered trajectories sterically impair H1 binding to the stacked nucleosomes in our structures. As the NRL increases, linker DNA trajectories relax, enabling H1 contacts and binding. Our results provide an explanation for why arrays with short NRLs are depleted of H1 and suited for transcription, whereas arrays with long NRLs show full H1 occupancy and can form transcriptionally silent heterochromatin regions. | ||
Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory.,Dombrowski M, Engeholm M, Dienemann C, Dodonova S, Cramer P Nat Struct Mol Biol. 2022 May;29(5):493-501. doi: 10.1038/s41594-022-00768-w., Epub 2022 May 17. PMID:35581345<ref>PMID:35581345</ref> | Histone H1 binding to nucleosome arrays depends on linker DNA length and trajectory.,Dombrowski M, Engeholm M, Dienemann C, Dodonova S, Cramer P Nat Struct Mol Biol. 2022 May;29(5):493-501. doi: 10.1038/s41594-022-00768-w. , Epub 2022 May 17. PMID:35581345<ref>PMID:35581345</ref> | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 7pf3" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 7pf3" style="background-color:#fffaf0;"></div> | ||
==See Also== | |||
*[[Histone 3D structures|Histone 3D structures]] | |||
== References == | == References == | ||
<references/> | <references/> | ||