Unraveling linker histone interactions in nucleosomes

Hao F., Kale S., Dimitrov S., Hayes J. J.

Current Opinion in Structural Biology, vol.71, pp.87-93, 2021 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Review
  • Volume: 71
  • Publication Date: 2021
  • Doi Number: 10.1016/j.sbi.2021.06.001
  • Journal Name: Current Opinion in Structural Biology
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus, Academic Search Premier, Chemical Abstracts Core, EMBASE, INSPEC, MEDLINE
  • Page Numbers: pp.87-93
  • Dokuz Eylül University Affiliated: Yes


© 2021 Elsevier LtdConsiderable progress has been made recently in defining the interactions of linker histones (H1s) within nucleosomes. Major advancements include atomic resolution structures of the globular domain of full-length H1s 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.