7pev: Difference between revisions
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==== | ==Nucleosome stack of the 4x177 nucleosome array containing H1== | ||
<StructureSection load='7pev' size='340' side='right'caption='[[7pev]]' scene=''> | <StructureSection load='7pev' size='340' side='right'caption='[[7pev]], [[Resolution|resolution]] 6.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol= FirstGlance]. <br> | <table><tr><td colspan='2'>[[7pev]] is a 18 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=7PEV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PEV 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=7pev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pev OCA], [https://pdbe.org/7pev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pev RCSB], [https://www.ebi.ac.uk/pdbsum/7pev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pev ProSAT]</span></td></tr> | </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=7pev FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pev OCA], [https://pdbe.org/7pev PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pev RCSB], [https://www.ebi.ac.uk/pdbsum/7pev PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pev ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/H32_HUMAN H32_HUMAN]] | |||
<div style="background-color:#fffaf0;"> | |||
== 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. | |||
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> | |||
</div> | |||
<div class="pdbe-citations 7pev" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Synthetic construct]] | ||
[[Category: Cramer P]] | |||
[[Category: Dombrowski M]] | |||
Revision as of 06:09, 8 September 2022
Nucleosome stack of the 4x177 nucleosome array containing H1Nucleosome stack of the 4x177 nucleosome array containing H1
Structural highlights
FunctionPublication Abstract from PubMedThroughout 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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