RPA binds histone H3-H4 and functions in DNA replication-coupled nucleosome assembly

被引：60
|
作者：
Liu, Shaofeng [1 ,2 ,3 ]
Xu, Zhiyun [1 ,2 ]
Leng, He [1 ,2 ,4 ]
Zheng, Pu [1 ,2 ]
Yang, Jiayi [1 ,2 ]
Chen, Kaifu [5 ]
Feng, Jianxun [1 ,2 ]
Li, Qing [1 ,2 ]
机构：
[1] Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China
[2] Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China
[3] Tsinghua Univ, Sch Life Sci, Peking Univ Tsinghua Univ Natl Inst Biol Sci Join, Beijing 100084, Peoples R China
[4] Peking Univ, Acad Adv Interdisciplinary Studies, Beijing 100871, Peoples R China
[5] Houston Methodist, DeBakey Heart & Vasc Ctr, Ctr Cardiovasc Regenerat, Houston, TX 77030 USA
来源：
SCIENCE | 2017年 / 355卷 / 6323期
基金：
中国国家自然科学基金;
关键词：
SINGLE-STRANDED-DNA; DAMAGE RESPONSE; CHROMATIN; YEAST; ACETYLATION; INHERITANCE; INVITRO; PROTEIN;
D O I：
10.1126/science.aah4712
中图分类号：
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号：
07 ; 0710 ; 09 ;
摘要：
DNA replication-coupled nucleosome assembly is essential to maintain genome integrity and retain epigenetic information. Multiple involved histone chaperones have been identified, but how nucleosome assembly is coupled to DNA replication remains elusive. Here we show that replication protein A (RPA), an essential replisome component that binds single-stranded DNA, has a role in replication-coupled nucleosome assembly. RPA directly binds free H3-H4. Assays using a synthetic sequence that mimics freshly unwound single-stranded DNA at replication fork showed that RPA promotes DNA-(H3-H4) complex formation immediately adjacent to double-stranded DNA. Further, an RPA mutant defective in H3-H4 binding exhibited attenuated nucleosome assembly on nascent chromatin. Thus, we propose that RPA functions as a platform for targeting histone deposition to replication fork, through which RPA couples nucleosome assembly with ongoing DNA replication.
引用
收藏
页码：415 / 419
页数：5
相关论文
共 50 条
  • [1] A Sequence in the Drosophila H3-H4 Promoter Triggers Histone Locus Body Assembly and Biosynthesis of Replication-Coupled Histone mRNAs
    Salzler, Harmony R.
    Tatomer, Deirdre C.
    Malek, Pamela Y.
    McDaniel, Stephen L.
    Orlando, Anna N.
    Marzluff, William F.
    Duronio, Robert J.
    [J]. DEVELOPMENTAL CELL, 2013, 24 (06) : 623 - 634
  • [2] Acetylation of histone H3 lysine 56 regulates replication-coupled nucleosome assembly
    Li, Qing
    Zhou, Hui
    Wurtele, Hugo
    Davies, Brian
    Horazdovsky, Bruce
    Verreault, Alain
    Zhang, Zhiguo
    [J]. CELL, 2008, 134 (02) : 244 - 255
  • [3] The Histone Chaperone FACT Contributes to DNA Replication-Coupled Nucleosome Assembly
    Yang, Jiayi
    Zhang, Xu
    Feng, Jianxun
    Leng, He
    Li, Shuqi
    Xiao, Junyu
    Liu, Shaofeng
    Xu, Zhiyun
    Xu, Jiawei
    Li, Di
    Wang, Zhongshi
    Wang, Jingyang
    Li, Qing
    [J]. CELL REPORTS, 2016, 14 (05): : 1128 - 1141
  • [4] The Role of Histone Modification in DNA Replication-Coupled Nucleosome Assembly and Cancer
    Zhang, Yaguang
    Zhang, Qin
    Zhang, Yang
    Han, Junhong
    [J]. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES, 2023, 24 (05)
  • [5] DNA polymerase δ subunit Pol32 binds histone H3-H4 and couples nucleosome assembly with Okazaki fragment processing
    Shi, Guojun
    Yang, Chaoqi
    Wu, Jiale
    Lei, Yang
    Hu, Jiazhi
    Feng, Jianxun
    Li, Qing
    [J]. SCIENCE ADVANCES, 2024, 10 (32):
  • [6] Roles of histone chaperones for DNA replication-coupled nucleosome assembly in Xenopus early embryos
    Shintomi, Keishi
    Kishimoto, Takeo
    Ohsumi, Keita
    [J]. ZOOLOGICAL SCIENCE, 2005, 22 (12) : 1457 - 1457
  • [7] Partitioning of Histone H3-H4 Tetramers During DNA Replication-Dependent Chromatin Assembly
    Xu, Mo
    Long, Chengzu
    Chen, Xiuzhen
    Huang, Chang
    Chen, She
    Zhu, Bing
    [J]. SCIENCE, 2010, 328 (5974) : 94 - 98
  • [8] Folding mechanism of the (H3-H4)2 histone tetramer of the core nucleosome
    Banks, DD
    Gloss, LM
    [J]. PROTEIN SCIENCE, 2004, 13 (05) : 1304 - 1316
  • [9] RPA functions as a platform for coupling of nucleosome assembly to DNA replication
    [J]. Science Foundation in China, 2017, (02) : 19 - 19
  • [10] NUCLEOSOME STRUCTURE .1. ALL 4 HISTONES, HISTONE-H2A, HISTONE-H2B, AND HISTONE-H4, ARE REQUIRED TO FORM A NUCLEOSOME, BUT AN H3-H4 SUBNUCLEOSOMAL PARTICLE IS FORMED WITH H3-H4 ALONE
    OUDET, P
    GERMOND, JE
    SURES, M
    GALLWITZ, D
    BELLARD, M
    CHAMBON, P
    [J]. COLD SPRING HARBOR SYMPOSIA ON QUANTITATIVE BIOLOGY, 1977, 42 : 287 - 300
12345