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
[1]   Structural evidence for Nap1-dependent H2A-H2B deposition and nucleosome assembly [J].
Aguilar-Gurrieri, Carmen ;
Larabi, Amede ;
Vinayachandran, Vinesh ;
Patel, Nisha A. ;
Yen, Kuangyu ;
Reja, Rohit ;
Ebong, Ima-O ;
Schoehn, Guy ;
Robinson, Carol V. ;
Pugh, B. Franklin ;
Panne, Daniel .
EMBO JOURNAL, 2016, 35 (13) :1465-1482
[2]   Chromatin replication and epigenome maintenance [J].
Alabert, Constance ;
Groth, Anja .
NATURE REVIEWS MOLECULAR CELL BIOLOGY, 2012, 13 (03) :153-167
[3]   The Histone Chaperone Nap1 Promotes Nucleosome Assembly by Eliminating Nonnucleosomal Histone DNA Interactions [J].
Andrews, Andrew J. ;
Chen, Xu ;
Zevin, Alexander ;
Stargell, Laurie A. ;
Luger, Karolin .
MOLECULAR CELL, 2010, 37 (06) :834-842
[4]   Histone Chaperones: Modulators of Chromatin Marks [J].
Avvakumov, Nikita ;
Nourani, Amine ;
Cote, Jacques .
MOLECULAR CELL, 2011, 41 (05) :502-514
[5]   Human Xip1 (C2orf13) is a novel regulator of cellular responses to DNA strand breaks [J].
Bekker-Jensen, Simon ;
Fugger, Kasper ;
Danielsen, Jannie Rendtlew ;
Gromova, Irina ;
Sehested, Maxwell ;
Celis, Julio ;
Bartek, Jiri ;
Lukas, Jiri ;
Mailand, Niels .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (27) :19638-19643
[6]   FACT facilitates transcription-dependent nucleosome alteration [J].
Belotserkovskaya, R ;
Oh, S ;
Bondarenko, VA ;
Orphanides, G ;
Studitsky, VM ;
Reinberg, D .
SCIENCE, 2003, 301 (5636) :1090-1093
[7]   The mammalian YL1 protein is a shared subunit of the TRRAP/TIP60 histone acetyltransferase and SRCAP complexes [J].
Cai, Y ;
Jin, JJ ;
Florens, L ;
Swanson, SK ;
Kusch, T ;
Li, B ;
Workman, JL ;
Washburn, MP ;
Conaway, RC ;
Conaway, JW .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (14) :13665-13670
[8]   Analysis of the Histone H3.1 Interactome: A Suitable Chaperone for the Right Event [J].
Campos, Eric I. ;
Smits, Arne H. ;
Kang, Young-Hoon ;
Landry, Sebastien ;
Escobar, Thelma M. ;
Nayak, Shruti ;
Ueberheide, Beatrix M. ;
Durocher, Daniel ;
Vermeulen, Michiel ;
Hurwitz, Jerard ;
Reinberg, Danny .
MOLECULAR CELL, 2015, 60 (04) :697-709
[9]   The program for processing newly synthesized histones H3.1 and H4 [J].
Campos, Eric I. ;
Fillingham, Jeffrey ;
Li, Guohong ;
Zheng, Haiyan ;
Voigt, Philipp ;
Kuo, Wei-Hung W. ;
Seepany, Harshika ;
Gao, Zhonghua ;
Day, Loren A. ;
Greenblatt, Jack F. ;
Reinberg, Danny .
NATURE STRUCTURAL & MOLECULAR BIOLOGY, 2010, 17 (11) :1343-U201
[10]   The SET protein regulates G2/M transition by modulating cyclin B-cyclin-dependent kinase 1 activity [J].
Canela, N ;
Rodriguez-Vilarrupla, A ;
Estanyol, JM ;
Díaz, C ;
Pujol, MJ ;
Agell, N ;
Bachs, O .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (02) :1158-1164