The unwrapping two turns of DNA on Chd1-bound nucleosomes cause the histone H3 tail and ubiquitin to be re-positioned.

Computational analysis of MNase-seq data reveals that alternatively positioned nucleosomes are prevalent in both yeast and human cells and create significant heterogeneity within cell populations.

Cooperative association of a histone-binding complex with pairs of appropriately modified nucleosomes, which form fundamental units of binding, mediates selective heterochromatin assembly and spreading.

Nucleosomes provide a direct and profound block to the activity of the CRISPR effector protein Cas9, suggesting future sophisticated design rules for CRISPR targeting.

Nucleosomes and linker histones block eukaryotic cytosine methylation.

In contrast to other transcription factors, CTCF and Esrrb rapidly regain binding after replication and remain bound to their targets during mitosis, preserving local nucleosome organization throughout the cell cycle.

NMR spectroscopy, dCypher assays, and CUT&RUN demonstrate that occlusion of the histone tails in the nucleosome context alters histone PTM specificity for a tandem of reader domains.

A computational method has been developed for predicting the cell-type-specific binding of transcription factors to nucleosomes, and involves integration of ChIP-seq, MNase-seq, and DNase-seq data with details of nucleosome structure.

Direct observation of RNA Polymerase II transcription through a single nucleosome at near basepair resolution suggests a mechanism for selective control of gene expression.

Structural models of the chromatin remodeling enzyme Chd1 in solution and when bound to chromatin indicate that conformational changes to both the enzyme and the nucleosome occur upon nucleotide dependent engagement.