title: Divergent Residues Within Histone H3 Dictate a Unique Chromatin Structure in Saccharomyces cerevisiae.
abstract: Histones are among the most conserved proteins known, but organismal differences do exist. In this study, we examined the contribution that divergent amino acids within histone H3 make to cell growth and chromatin structure in Saccharomyces cerevisiae. We show that, while amino acids that define histone H3.3 are dispensable for yeast growth, substitution of residues within the histone H3 α3 helix with human counterparts results in a severe growth defect. Mutations within this domain also result in altered nucleosome positioning, both in vivo and in vitro, which is accompanied by increased preference for nucleosome-favoring sequences. These results suggest that divergent amino acids within the histone H3 α3 helix play organismal roles in defining chromatin structure.
authors.affiliation: Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
authors.forename: Kristina L
authors.initials: KL
authors.lastname: McBurney
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada V8P 5C2.
authors.forename: Andrew
authors.initials: A
authors.lastname: Leung
authors.affiliation: Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
authors.forename: Jennifer K
authors.initials: JK
authors.lastname: Choi
authors.affiliation: Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
authors.forename: Benjamin J E
authors.initials: BJ
authors.lastname: Martin
authors.affiliation: Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3.
authors.forename: Nicholas A T
authors.initials: NA
authors.lastname: Irwin
authors.affiliation: Chromatin Biochemistry Group, Medical Research Council Clinical Sciences Centre, Imperial College London, London, W12 0NN, United Kingdom.
authors.forename: Till
authors.initials: T
authors.lastname: Bartke
authors.affiliation: Department of Biochemistry and Microbiology, University of Victoria, Victoria, British Columbia, Canada V8P 5C2.
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Nelson
authors.affiliation: Department of Biochemistry and Molecular Biology, University of British Columbia, Vancouver, British Columbia, Canada V6T 1Z3 ljhowe@mail.ubc.ca.
authors.forename: LeAnn J
authors.initials: LJ
authors.lastname: Howe
mesh_terms: D000595:Amino Acid Sequence; D019943:Amino Acid Substitution; D002843:Chromatin / Q000737:chemistry*; D006657:Histones / Q000737:chemistry*; D006801:Humans; D008969:Molecular Sequence Data; D009707:Nucleosomes; D011994:Recombinant Proteins; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000254:growth & development / Q000648:ultrastructure*
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D011994:Recombinant Proteins
keywords: H3; S. cerevisiae; histone; nucleosome positioning