title: Histone H4, the cell cycle and a question of integrity.
abstract: The N-terminal domain of histone H4 has been implicated in various nuclear functions, including gene silencing and activation and replication-linked chromatin assembly. Many of these have been identified by using h4 mutants in the yeast S. cerevisiae. In a recent paper, Megee et al. use this approach to show that mutants in which all four N-terminal H4 lysines are substituted with glutamines accumulate increased levels of DNA damage. A single lysine, but not an arginine, anywhere in the N-terminal domain suppresses this phenotype. It is suggested that histone H4 plays a role in maintaining genome integrity through the cell cycle, possibly by a mechanism involving lysine acetylation.
authors.affiliation: Anatomy Department, University of Birmingham Medical School, Edgbaston, UK.
authors.forename: B M
authors.initials: BM
authors.lastname: Turner
mesh_terms: D000595:Amino Acid Sequence; D002453:Cell Cycle / Q000502:physiology*; D004249:DNA Damage; D006657:Histones / Q000502:physiology*; D008969:Molecular Sequence Data; D012441:Saccharomyces cerevisiae / Q000166:cytology
chemical_list: D006657:Histones