Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2  被引量:2

Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2

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作  者:Hong Wang (1) (2)  Mingzhu Wang (1)  Na Yang (1) (2)  Rui-Ming Xu (1) (2) 

机构地区:[1]1.National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing, 100101, China 2.University of Chinese Academy of Sciences, Beijing, 100049, China

出  处:《Protein & Cell》2015年第9期693-697,共5页蛋白质与细胞(英文版)

摘  要:The building block of eukaryotic chromatin is the nucleo- some core particle (NCP), which is consisted of -146 bps of DNA wrapped around an octamer of core histones. A tetra- mer of histone H3 and H4 and two H2A-H2B dimers form the histone octamer (Kornberg, 1974; Luger et al., 1997; Tho- mas and Kornberg, 1975). During DNA replication, nucleo- some disassembly and reassembly occurs at the replication fork, and histone chaperons CAF-1 and ASF1 are principally responsible for the deposition of histones H3 and H4 onto replicated DNA (Kaufman et al., 1995; Tyler et al., 1999). ASF1 binds a heterodimeric histone H3-H4 complex through its conserved N-terminal domain (aa 1-155) and impedes the formation of the (H3-H4)2 tetramer both inside the nucleus and in the cytoplasm (English et al., 2005).The building block of eukaryotic chromatin is the nucleo- some core particle (NCP), which is consisted of -146 bps of DNA wrapped around an octamer of core histones. A tetra- mer of histone H3 and H4 and two H2A-H2B dimers form the histone octamer (Kornberg, 1974; Luger et al., 1997; Tho- mas and Kornberg, 1975). During DNA replication, nucleo- some disassembly and reassembly occurs at the replication fork, and histone chaperons CAF-1 and ASF1 are principally responsible for the deposition of histones H3 and H4 onto replicated DNA (Kaufman et al., 1995; Tyler et al., 1999). ASF1 binds a heterodimeric histone H3-H4 complex through its conserved N-terminal domain (aa 1-155) and impedes the formation of the (H3-H4)2 tetramer both inside the nucleus and in the cytoplasm (English et al., 2005).

分 类 号:Q523[生物学—生物化学] S511[农业科学—作物学]

 

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