7pfc: Difference between revisions
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==== | ==Nucleosome stack of the 4x197 nucleosome array containing H1== | ||
<StructureSection load='7pfc' size='340' side='right'caption='[[7pfc]]' scene=''> | <StructureSection load='7pfc' size='340' side='right'caption='[[7pfc]], [[Resolution|resolution]] 6.40Å' 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'>[[7pfc]] is a 19 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=7PFC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7PFC 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=7pfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pfc OCA], [https://pdbe.org/7pfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pfc RCSB], [https://www.ebi.ac.uk/pdbsum/7pfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pfc 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=7pfc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7pfc OCA], [https://pdbe.org/7pfc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7pfc RCSB], [https://www.ebi.ac.uk/pdbsum/7pfc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7pfc ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[https://www.uniprot.org/uniprot/H2B1K_HUMAN H2B1K_HUMAN]] 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. Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. | |||
<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 7pfc" 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 4x197 nucleosome array containing H1Nucleosome stack of the 4x197 nucleosome array containing H1
Structural highlights
Function[H2B1K_HUMAN] 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. Has broad antibacterial activity. May contribute to the formation of the functional antimicrobial barrier of the colonic epithelium, and to the bactericidal activity of amniotic fluid. Publication 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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