Aug 2026· Biomolecules· Vol 16, pp. 1181· 0 citations· 92 references
Medicine
TL;DR
This review introduces the basics of chromatin structure, what is known about how linker histones (H1s) bind to nucleosomes and influence chromatin, and how the individual domains within H1s contribute to these activities.
Abstract
Chromatin structure is dynamic and regulated by many factors, including enzymes that chemically modify histones and DNA, chromatin remodeling complexes that physically manipulate nucleosomes and chromatin, and non-enzymatic proteins that bind to DNA or nucleosomes to create specialized regions in chromatin. This multifactorial regulation stems from the need for fine-tuned control, which is key in processes including DNA repair, replication, and gene expression. Linker histones are a family of proteins structurally distinct from the core histones that provide a poorly understood layer of regulation in chromatin. In this review, we introduce the basics of chromatin structure, what is known about how linker histones (H1s) bind to nucleosomes and influence chromatin, and how the individual domains within H1s contribute to these activities. We especially focus on recent studies describing canonical and alternative H1-nucleosome binding and their potential roles in chromatin.
Current advances in understanding the molecular mechanisms by which human and yeast CAF-1 complexes are recruited to sites of DNA synthesis and how CAF-1 function is coordinated with other histone chaperones during replication and repair are summarized.
Ian P. Hall, Carly A. Nowoj, Lynne M. Dieckman· Biomolecules· 0 citations
Nucleosomes integrate diverse histone variants to organize chromatin and coordinate genome maintenance. In plants, the structural interplay between replication-associated histones and DNA damage-responsive histone variants remains poorly understood. Here, we determine cryogenic electron microscopy structures of an Arab...
Rashmi Panigrahi, Ross A. Edwards, Nathaniel Agbagba et al.· Cells· 0 citations
A proximity-labeling protocol for identifying the chromatin-dependent protein interactome associated with specific chromatin marks, termed ChromID, which preserves native chromatin organization and captures transient chromatin-associated interactions that are often lost during conventional affinity purification workflo...
Richard Cardoso da Silva, Douwe ten Bulte, T. Baubec· Bio-protocol· 0 citations
Linker histone H1 is an essential chromatin architectural protein that compacts chromatin into transcriptionally silent regions by interacting with nucleosomal and linker DNA while rapidly exchanging in vivo. How H1 targets nucleosomes while being dynamic remains unanswered. Using a single-molecule strategy, we investi...
E. Akbari, Nathaniel L. Burge, M. Valdimarsson et al.· Molecules and Cells· 0 citations
The six-residue loop 2 of H2A and H2A is used to map, at single-residue resolution, how nucleosome-core variation reshapes cellular function, and identifies histone variation as a source of phenotypic innovation.
Zachary H. Harvey, Benjamin Gundinger, Jian-Yi Kok et al.· bioRxiv· 0 citations
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