Histone structure and nucleosome stability

被引：215
作者：
Marino-Ramirez, Leonardo
Kann, Maricel G.
Shoemaker, Benjamin A.
Landsman, David
机构：
[1] Natl Lib Med, NIH, Computat Biol Branch, Natl Ctr Biotechnol Informat, Bethesda, MD 20894 USA
[2] Natl Lib Med, NIH, Computat Biol Branch, Natl Ctr Biotechnol Informat, Bethesda, MD 20894 USA
来源：
EXPERT REVIEW OF PROTEOMICS | 2005年 / 2卷 / 05期
关键词：
chromatin structure; historic variants; nucleosomes;
D O I：
10.1586/14789450.2.5.719
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Histone proteins play essential structural and functional roles in the transition between active and inactive chromatin states. Although histones have a high degree of conservation due to constraints to maintain the overall structure of the nucleosomal octameric core, variants have evolved to assume diverse roles in gene regulation and epigenetic silencing. Histone variants, post-translational modifications and interactions with chromatin remodeling complexes influence DNA replication, transcription, repair and recombination. The authors review recent findings on the structure of chromatin that confirm previous interparticle interactions observed in crystal structures.
引用
收藏
页码：719 / 729
页数：11
相关论文
共 72 条
[1]   The histone variant H3.3 marks active chromatin by replication-independent nucleosome assembly [J].
Ahmad, K ;
Henikoff, S .
MOLECULAR CELL, 2002, 9 (06) :1191-1200
[2]   Identification and characterization of the Drosophila histone h4 replacement gene [J].
Akhmanova, A ;
Miedema, K ;
Hennig, W .
FEBS LETTERS, 1996, 388 (2-3) :219-222
[3]  
Albig W, 1996, HUM GENET, V97, P486
[4]   The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling [J].
Angelov, D ;
Molla, A ;
Perche, PY ;
Hans, F ;
Côté, J ;
Khochbin, S ;
Bouvet, P ;
Dimitrov, S .
MOLECULAR CELL, 2003, 11 (04) :1033-1041
[5]   THE HISTONE FOLD - A UBIQUITOUS ARCHITECTURAL MOTIF UTILIZED IN DNA COMPACTION AND PROTEIN DIMERIZATION [J].
ARENTS, G ;
MOUDRIANAKIS, EN .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1995, 92 (24) :11170-11174
[6]   The major subacrosomal occupant of bull spermatozoa is a novel histone H2B variant associated with the forming acrosome during spermiogenesis (vol 239, pg 376, 2001) [J].
Aul, RB ;
Oko, RJ .
DEVELOPMENTAL BIOLOGY, 2002, 242 (02) :268-280
[7]   Nucleosomes containing the histone variant H2A.Bbd organize only 118 base pairs of DNA [J].
Bao, YH ;
Konesky, K ;
Park, YJ ;
Rosu, S ;
Dyer, PN ;
Rangasamy, D ;
Tremethick, DJ ;
Laybourn, PJ ;
Luger, K .
EMBO JOURNAL, 2004, 23 (16) :3314-3324
[8]   A VARIETY OF DNA-BINDING AND MULTIMERIC PROTEINS CONTAIN THE HISTONE FOLD MOTIF [J].
BAXEVANIS, AD ;
ARENTS, G ;
MOUDRIANAKIS, EN ;
LANDSMAN, D .
NUCLEIC ACIDS RESEARCH, 1995, 23 (14) :2685-2691
[9]   Specific contributions of histone tails and their acetylation to the mechanical stability of nucleosomes [J].
Brower-Toland, B ;
Wacker, DA ;
Fulbright, RM ;
Lis, JT ;
Kraus, WL ;
Wang, MD .
JOURNAL OF MOLECULAR BIOLOGY, 2005, 346 (01) :135-146
[10]   Histone H2AX phosphorylation is dispensable for the initial recognition of DNA breaks [J].
Celeste, A ;
Fernandez-Capetillo, O ;
Kruhlak, MJ ;
Pilch, DR ;
Staudt, DW ;
Lee, A ;
Bonner, RF ;
Bonner, WM ;
Nussenzweig, A .
NATURE CELL BIOLOGY, 2003, 5 (07) :675-U51
12345678