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XB-ART-58517
Nat Commun 2021 Sep 06;121:5280. doi: 10.1038/s41467-021-25568-6.
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Binding of regulatory proteins to nucleosomes is modulated by dynamic histone tails.

Peng Y , Li S , Onufriev A , Landsman D , Panchenko AR .


Abstract
Little is known about the roles of histone tails in modulating nucleosomal DNA accessibility and its recognition by other macromolecules. Here we generate extensive atomic level conformational ensembles of histone tails in the context of the full nucleosome, totaling 65 microseconds of molecular dynamics simulations. We observe rapid conformational transitions between tail bound and unbound states, and characterize kinetic and thermodynamic properties of histone tail-DNA interactions. Different histone types exhibit distinct binding modes to specific DNA regions. Using a comprehensive set of experimental nucleosome complexes, we find that the majority of them target mutually exclusive regions with histone tails on nucleosomal/linker DNA around the super-helical locations ± 1, ± 2, and ± 7, and histone tails H3 and H4 contribute most to this process. These findings are explained within competitive binding and tail displacement models. Finally, we demonstrate the crosstalk between different histone tail post-translational modifications and mutations; those which change charge, suppress tail-DNA interactions and enhance histone tail dynamics and DNA accessibility.

PubMed ID: 34489435
Article link: Nat Commun
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2bc21 ino80 smarca5
GO keywords: chromatin [+]


Article Images: [+] show captions
References [+] :
Allahverdi, The effects of histone H4 tail acetylations on cation-induced chromatin folding and self-association. 2011, Pubmed