Unraveling linker histone interactions in nucleosomes

Considerable progress has been made recently in defining the interactions of linker histones (H1 s) within nucleosomes. Major advancements include atomic resolution structures of the globular domain of full-length 1-11 s in the context of nucleosomes containing full-length linker DNA. Although these studies have led to a detailed understanding of the interactions and dynamics of H1 globular domains in the canonical on-dyad nucleosome binding pocket, more information regarding the intrinsically disordered N-terminal and C-terminal domains is needed. In this review, we highlight studies supporting our current understanding of the structures and interactions of the N-terminal, globular, and C-terminal domains of linker histones within the nucleosome.

Automated summary

Significant progress has been made recently in defining the interactions of linker histones (H1 s) within nucleosomes, particularly in understanding the structures and interactions of the globular domains. However, more information is needed regarding the intrinsically disordered N-terminal and C-terminal domains.