title: Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility.
abstract: Although the archaeal and eukaryotic nucleosome core histones evolved from a common ancestor, conserved lysine residues are present at DNA-binding locations in all four eukaryotic histones that are not present in the archaeal histones. Introduction of lysine residues at the corresponding locations into an archaeal histone, HMfB, generated a variant with increased affinity for DNA that formed more compact complexes with DNA. However, these complexes no longer facilitated the circularization of short DNA molecules and had lost the flexibility to wrap DNA alternatively in either a negative or positive supercoil.
authors.affiliation: Department of Microbiology, The Ohio State University, Columbus, Ohio 43210-1292, USA.
authors.forename: Divya J
authors.initials: DJ
authors.lastname: Soares
authors.forename: Frédéric
authors.initials: F
authors.lastname: Marc
authors.forename: John N
authors.initials: JN
authors.lastname: Reeve
mesh_terms: D000595:Amino Acid Sequence; D019843:Archaeal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017124:Conserved Sequence; D004270:DNA, Circular / Q000378:metabolism; D005057:Eukaryotic Cells; D006657:Histones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009707:Nucleosomes / Q000737:chemistry; D017510:Protein Folding
chemical_list: D019843:Archaeal Proteins; D004270:DNA, Circular; D006657:Histones; D009707:Nucleosomes