title: Archaeal histones: structures, stability and DNA binding.
abstract: Structures, stability and DNA-binding properties have been established for archaeal histones from mesophiles, thermophiles and hyperthermophiles. Most archaeal histones are simply histone folds that are stabilized by dimer formation. Archaeal histones and the histone folds of the eukaryotic nucleosome core histones share a common ancestry and bind and wrap DNA similarly using conserved residues. The histone-fold residues that stabilize dimer-dimer interactions within an archaeal histone core contribute to determining archaeal histone-DNA affinity.
authors.affiliation: Department of Microbiology, Ohio State University, Columbus, OH 43210, U.S.A. reeve.2@osu.edu
authors.forename: J N
authors.initials: JN
authors.lastname: Reeve
authors.forename: K A
authors.initials: KA
authors.lastname: Bailey
authors.forename: W-T
authors.initials: WT
authors.lastname: Li
authors.forename: F
authors.initials: F
authors.lastname: Marc
authors.forename: K
authors.initials: K
authors.lastname: Sandman
authors.forename: D J
authors.initials: DJ
authors.lastname: Soares
mesh_terms: D000595:Amino Acid Sequence; D001105:Archaea / Q000737:chemistry / Q000235:genetics* / Q000502:physiology*; D002942:Circular Dichroism; D004247:DNA / Q000737:chemistry*; D019281:Dimerization; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006358:Hot Temperature; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry; D011489:Protein Denaturation; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
chemical_list: D006657:Histones; D009707:Nucleosomes; D004247:DNA