Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-58422
Mol Cell 2021 Nov 04;8121:4377-4397.e12. doi: 10.1016/j.molcel.2021.08.010.
Show Gene links Show Anatomy links

Structural features of nucleosomes in interphase and metaphase chromosomes.

Arimura Y , Shih RM , Froom R , Funabiki H .


Abstract
Structural heterogeneity of nucleosomes in functional chromosomes is unknown. Here, we devise the template-, reference- and selection-free (TRSF) cryo-EM pipeline to simultaneously reconstruct cryo-EM structures of protein complexes from interphase or metaphase chromosomes. The reconstructed interphase and metaphase nucleosome structures are on average indistinguishable from canonical nucleosome structures, despite DNA sequence heterogeneity, cell-cycle-specific posttranslational modifications, and interacting proteins. Nucleosome structures determined by a decoy-classifying method and structure variability analyses reveal the nucleosome structural variations in linker DNA, histone tails, and nucleosome core particle configurations, suggesting that the opening of linker DNA, which is correlated with H2A C-terminal tail positioning, is suppressed in chromosomes. High-resolution (3.4-3.5 Å) nucleosome structures indicate DNA-sequence-independent stabilization of superhelical locations ±0-1 and ±3.5-4.5. The linker histone H1.8 preferentially binds to metaphase chromatin, from which chromatosome cryo-EM structures with H1.8 at the on-dyad position are reconstituted. This study presents the structural characteristics of nucleosomes in chromosomes.

PubMed ID: 34478647
PMC ID: PMC8571072
Article link: Mol Cell
Grant support: [+]

Species referenced: Xenopus laevis
Genes referenced: h2ac21
GO keywords: nucleosome [+]


Article Images: [+] show captions
References [+] :
Adams, Binding of disparate transcriptional activators to nucleosomal DNA is inherently cooperative. 1995, Pubmed