Conserved eukaryotic histone-fold residues substituted into an archaeal histone increase DNA affinity but reduce complex flexibility.
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.
Soares
Divya J
DJ
Department of Microbiology, The Ohio State University, Columbus, Ohio 43210-1292, USA.
Marc
Frédéric
F
Reeve
John N
JN
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
D019843:Archaeal Proteins; D004270:DNA, Circular; D006657:Histones; D009707:Nucleosomes