title: Not just for coding: a new role for histone tails in replication enzyme activation.
abstract: The processing of Okazaki fragments when they are assembled into nucleosomes has received little attention. In this issue of The FEBS Journal, Seo and colleagues show that binding to histone tails stimulates the enzymatic activity of flap endonuclease 1 (Rad27). Histone tails are structurally similar to the C terminus of Rad27 and can thus mimic its autostimulatory function. This study highlights an active regulatory role for nucleosomes on DNA metabolism.
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA.
authors.forename: Anja-Katrin
authors.initials: AK
authors.lastname: Bielinsky
authors.affiliation: Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN, USA.
authors.forename: Wendy
authors.initials: W
authors.lastname: Leung
mesh_terms: D004247:DNA / Q000235:genetics; D004261:DNA Replication; D004789:Enzyme Activation; D045585:Flap Endonucleases / Q000235:genetics; D006657:Histones / Q000235:genetics*; D009707:Nucleosomes; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics*
chemical_list: D006657:Histones; D009707:Nucleosomes; D029701:Saccharomyces cerevisiae Proteins; D004247:DNA; D045585:Flap Endonucleases