Recent Progress in Histone Chaperones Associated With H2A-H2B Type Histones

被引:0
作者
Huang Yan [1 ,2 ]
Zhou Zheng [1 ]
机构
[1] Chinese Acad Sci, Inst Biophys, Beijing 100101, Peoples R China
[2] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
基金
中国国家自然科学基金;
关键词
H2A histone; histone variant; histone chaperone; chromatin structure; NUCLEOSOME ASSEMBLY PROTEIN-1; CHROMATIN-REMODELING COMPLEX; DNA STRAND BREAKS; STRUCTURAL BASIS; SACCHAROMYCES-CEREVISIAE; GENE-TRANSCRIPTION; NUCLEAR TRANSPORT; CRYSTAL-STRUCTURE; REMOVES H2A.Z; CORE PARTICLE;
D O I
10.16476/j.pibb.2018.0222
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Eukaryotic DNA that carries the genetic code is packaged into the chromatin. The dynamic structure of chromatin controls the accessibility of DNA in processes of DNA replication, transcription, recombination, and DNA damage repair. Histone, a fundamental component of chromatin, plays a central role in regulating the chromatin structure owing to its ability to introduce a large variety of histone variants and modifications. Compared to other core histones (H2B, H3 and H4), H2A type of histone contains the largest number of variants which increase the compositional and structural diversity of nucleosome and chromatin. A number of histone chaperones recognize and assist the H2A-H2B type of histones for their folding, modification, transportation, incorporation, and eviction. Here, we reviewed the recent progress in the molecular mechanisms by which histone chaperones recognize the H2A-H2B type of histones and function in control of the chromatin dynamics.
引用
收藏
页码:971 / 980
页数:10
相关论文
共 97 条
[51]   NUCLEOSOMES ARE ASSEMBLED BY AN ACIDIC PROTEIN WHICH BINDS HISTONES AND TRANSFERS THEM TO DNA [J].
LASKEY, RA ;
HONDA, BM ;
MILLS, AD ;
FINCH, JT .
NATURE, 1978, 275 (5679) :416-420
[52]   Molecular basis and specificity of H2A.Z-H2B recognition and deposition by the histone chaperone YL1 [J].
Latrick, Chrysa M. ;
Marek, Martin ;
Ouararhni, Khalid ;
Papin, Christophe ;
Stoll, Isabelle ;
Ignatyeva, Maria ;
Obri, Arnaud ;
Ennifar, Eric ;
Dimitrov, Stefan ;
Romier, Christophe ;
Hamiche, Ali .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2016, 23 (04) :309-316
[53]   The chromatin-remodeling factor FACT contributes to centromeric heterochromatin independently of RNAi [J].
Lejeune, Erwan ;
Bortfeld, Miriam ;
White, Sharon A. ;
Pidoux, Alison L. ;
Ekwall, Karl ;
Allshire, Robin C. ;
Ladurner, Andreas G. .
CURRENT BIOLOGY, 2007, 17 (14) :1219-1224
[54]   Histone release during transcription: NAP1 forms a complex with H2A and H2B and facilitates a topologically dependent release of H3 and H4 from the nucleosome [J].
Levchenko, V ;
Jackson, V .
BIOCHEMISTRY, 2004, 43 (09) :2359-2372
[55]   FACT Remodels the Tetranucleosomal Unit of Chromatin Fibers for Gene Transcription [J].
Li, Wei ;
Chen, Ping ;
Yu, Juan ;
Dong, Liping ;
Liang, Dan ;
Feng, Jianxun ;
Yan, Jie ;
Wang, Peng-Ye ;
Li, Qing ;
Zhang, Zhiguo ;
Li, Ming ;
Li, Guohong .
MOLECULAR CELL, 2016, 64 (01) :120-133
[56]   Structural basis of H2A.Z recognition by SRCAP chromatin-remodeling subunit YL1 [J].
Liang, Xiaoping ;
Shan, Shan ;
Pan, Lu ;
Zhao, Jicheng ;
Ranjan, Anand ;
Wang, Feng ;
Zhang, Zhuqiang ;
Huang, Yingzi ;
Feng, Hanqiao ;
Wei, Debbie ;
Huang, Li ;
Liu, Xuehui ;
Zhong, Qiang ;
Lou, Jizhong ;
Li, Guohong ;
Wu, Carl ;
Zhou, Zheng .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2016, 23 (04) :317-323
[57]   Histone chaperone Chz1 facilitates the disfavouring property of Spt16 to H2A.Z-containing genes in Saccharomyces cerevisiae [J].
Liu, Hongde ;
Luo, Kun ;
Zhou, Zikai ;
Mu, Yawen ;
Wan, Yakun .
BIOCHEMICAL JOURNAL, 2014, 460 :387-397
[58]   Crystal structure of the nucleosome core particle at 2.8 angstrom resolution [J].
Luger, K ;
Mader, AW ;
Richmond, RK ;
Sargent, DF ;
Richmond, TJ .
NATURE, 1997, 389 (6648) :251-260
[59]   Chz1, a nuclear chaperone for histone H2AZ [J].
Luk, Ed ;
Vu, Ngoc-Diep ;
Patteson, Kern ;
Mizuguchi, Gaku ;
Wu, Wei-Hua ;
Ranjan, Anand ;
Backus, Jonathon ;
Sen, Subhojit ;
Lewis, Marc ;
Bai, Yawen ;
Wu, Carl .
MOLECULAR CELL, 2007, 25 (03) :357-368
[60]   Stepwise Histone Replacement by SWR1 Requires Dual Activation with Histone H2A.Z and Canonical Nucleosome [J].
Luk, Ed ;
Ranjan, Anand ;
FitzGerald, Peter C. ;
Mizuguchi, Gaku ;
Huang, Yingzi ;
Wei, Debbie ;
Wu, Carl .
CELL, 2010, 143 (05) :725-736