title: Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.
abstract: Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 A crystal structure of the core domain of Rtt106p, which adopts an unusual "double pleckstrin homology" domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Yiwei
authors.initials: Y
authors.lastname: Liu
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Hongda
authors.initials: H
authors.lastname: Huang
authors.affiliation: the State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Graduate School, Chinese Academy of Sciences, Shanghai 200031, China.
authors.forename: Bo O
authors.initials: BO
authors.lastname: Zhou
authors.affiliation: the State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Graduate School, Chinese Academy of Sciences, Shanghai 200031, China.
authors.forename: Shan-Shan
authors.initials: SS
authors.lastname: Wang
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Yingxia
authors.initials: Y
authors.lastname: Hu
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Xu
authors.initials: X
authors.lastname: Li
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Jianping
authors.initials: J
authors.lastname: Liu
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Jianye
authors.initials: J
authors.lastname: Zang
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Liwen
authors.initials: L
authors.lastname: Niu
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and.
authors.forename: Jihui
authors.initials: J
authors.lastname: Wu
authors.affiliation: the State Key Laboratory of Molecular Biology, Institute of Biochemistry and Cell Biology, Shanghai Institutes for Biological Sciences, the Graduate School, Chinese Academy of Sciences, Shanghai 200031, China.
authors.forename: Jin-Qiu
authors.initials: JQ
authors.lastname: Zhou
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and. Electronic address: mkteng@ustc.edu.cn.
authors.forename: Maikun
authors.initials: M
authors.lastname: Teng
authors.affiliation: From the Hefei National Laboratory for Physical Sciences at Microscale and School of Life Science, University of Science and Technology of China, Hefei, Anhui 230026 and. Electronic address: yyshi@ustc.edu.cn.
authors.forename: Yunyu
authors.initials: Y
authors.lastname: Shi
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D015153:Blotting, Western; D018360:Crystallography, X-Ray; D004271:DNA, Fungal / Q000235:genetics / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D015966:Gene Expression Regulation, Fungal; D006570:Heterochromatin / Q000235:genetics*; D006657:Histones / Q000378:metabolism; D008954:Models, Biological; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D009154:Mutation; D009707:Nucleosomes / Q000378:metabolism; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D017386:Sequence Homology, Amino Acid; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism
chemical_list: D004271:DNA, Fungal; D004268:DNA-Binding Proteins; D006570:Heterochromatin; D006657:Histones; D018832:Molecular Chaperones; D009707:Nucleosomes; C505157:Rtt106 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D038281:Silent Information Regulator Proteins, Saccharomyces cerevisiae