Cracking the enigmatic linker histone code

被引:39
作者
Godde, James S. [1 ,2 ]
Ura, Kiyoe [1 ]
机构
[1] Osaka Univ, Grad Sch Med, Div Gen Therapy Sci, Suita, Osaka 5650871, Japan
[2] Monmouth Coll, Dept Biol, Monmouth, IL 61462 USA
关键词
epigenetic code; histone H1; histone modification; histone variant; linker histone;
D O I
10.1093/jb/mvn013
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
Recently, the existence of a 'histone code' has been proposed to explain the link between the covalent chemical modification of histone proteins and the epigenetic regulation of gene activity. Although the role of the four 'core' histones has been extensively studied, little is known about the involvement of the linker histone, histone H1 and its variants, in this code. For many years, few sites of chemical modification had been mapped in linker histones, but this has changed recently with the use of functional proteomic techniques, principally mass spectrometry, to characterize these modifications. The functionality of many of these sites, however, remains to be determined.
引用
收藏
页码:287 / 293
页数:7
相关论文
共 51 条
[1]  
Ausió J, 2000, BIOESSAYS, V22, P873, DOI 10.1002/1521-1878(200010)22:10<873::AID-BIES1>3.0.CO
[2]  
2-R
[3]  
Ausio Juan, 2006, Briefings in Functional Genomics & Proteomics, V5, P228, DOI 10.1093/bfgp/ell020
[4]   Histone H1 is dispensable for methylation-associated gene silencing in Ascobolus immersus and essential for long life span [J].
Barra, JL ;
Rhounim, L ;
Rossignol, JL ;
Faugeron, G .
MOLECULAR AND CELLULAR BIOLOGY, 2000, 20 (01) :61-69
[5]  
Brown SJ, 2001, NYU SA CTR SER F M I, V6, P1
[6]   The dynamics of histone H1 function in chromatin [J].
Bustin, M ;
Catez, F ;
Lim, JH .
MOLECULAR CELL, 2005, 17 (05) :617-620
[7]   HOMONUCLEAR AND HETERONUCLEAR 2-DIMENSIONAL NMR-STUDIES OF THE GLOBULAR DOMAIN OF HISTONE H1 - FULL ASSIGNMENT, TERTIARY STRUCTURE, AND COMPARISON WITH THE GLOBULAR DOMAIN OF HISTONE H5 [J].
CERF, C ;
LIPPENS, G ;
RAMAKRISHNAN, V ;
MUYLDERMANS, S ;
SEGERS, A ;
WYNS, L ;
WODAK, SJ ;
HALLENGA, K .
BIOCHEMISTRY, 1994, 33 (37) :11079-11086
[8]   HP1 binds specifically to Lys26-methylated histone H1.4, whereas simultaneous Ser27 phosphorylation blocks HP1 binding [J].
Daujat, S ;
Zeissler, U ;
Waldmann, T ;
Happel, N ;
Schneider, R .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2005, 280 (45) :38090-38095
[9]   Understanding global changes in histone H1 phosphorylation using mass spectrometry [J].
Deterding, LJ ;
Banks, GC ;
Tomer, KB ;
Archer, TK .
METHODS, 2004, 33 (01) :53-58
[10]   Suppression of homologous recombination by the Saccharomyces cerevisiae linker histone [J].
Downs, JA ;
Kosmidou, E ;
Morgan, A ;
Jackson, SP .
MOLECULAR CELL, 2003, 11 (06) :1685-1692