title: Molecular dynamics of histone H1.
abstract: The H1 or linker histones bind dynamically to chromatin in living cells via a process that involves transient association with the nucleosome near the DNA entry/exit site followed by dissociation, translocation to a new location, and rebinding. The mean residency time of H1 on any given nucleosome is about a minute, which is much shorter than that of most core histones but considerably longer than that of most other chromatin-binding proteins, including transcription factors. Here we review recent advances in understanding the kinetic pathway of H1 binding and how it relates to linker histone structure and function. We also describe potential mechanisms by which the dynamic binding of H1 might contribute directly to the regulation of gene expression and discuss several situations for which there is experimental evidence to support these mechanisms. Finally, we review the evidence for the participation of linker histone chaperones in mediating H1 exchange.
authors.affiliation: Department of Biochemistry, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, USA.
authors.forename: Thomas W
authors.initials: TW
authors.lastname: Flanagan
authors.affiliation: Department of Biochemistry, University of Mississippi Medical Center, 2500 North State Street, Jackson, MS 39216, USA. Electronic address: dbrown@umc.edu.
authors.forename: David T
authors.initials: DT
authors.lastname: Brown
mesh_terms: D000818:Animals; D005786:Gene Expression Regulation; D056488:Histone Chaperones / Q000502:physiology; D006657:Histones / Q000737:chemistry*; D006801:Humans; D056004:Molecular Dynamics Simulation
chemical_list: D056488:Histone Chaperones; D006657:Histones
keywords: Chromatin; FRAP; H1; Linker histone; Mobility; Nucleosome; Photobleaching