Histone structure and function.
The past year has seen major advances in our understanding of histone and nucleosome structure and function. Direct DNA mapping and thermodynamic experiments have finally provided conclusive evidence that the histones impose an altered helical pitch on the DNA as it is wrapped on the surface of the core histone octamer. Further, it is now clear that lysine acetylation in the amino-terminal domains of histones H3 and H4 can alter the topology of the DNA in chromatin and probably influence its higher-order folding. Genetic experiments reported in the past year have provided a wealth of new information on histone structure and function, including the identification of the peptide domain of histone H4 that is necessary for permanent gene repression, the confirmation that nucleosome structure is critical for centromere function, and evidence that histone acetylation plays a significant role in chromosome dynamics.
Smith
M M
MM
Department of Microbiology, School of Medicine, University of Virginia, Charlottesville 22908.
D000595:Amino Acid Sequence; D000818:Animals; D004247:DNA / Q000378:metabolism*; D006657:Histones / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D046911:Macromolecular Substances; D008961:Models, Structural; D008969:Molecular Sequence Data
D006657:Histones; D046911:Macromolecular Substances; D004247:DNA