Histone H2A ubiquitination does not preclude histone H1 binding, but it facilitates its association with the nucleosome

被引:38
作者
Jason, LJM
Finn, RM
Lindsey, G
Ausió, J
机构
[1] Univ Victoria, Dept Biochem & Microbiol, Victoria, BC V8W 396, Canada
[2] Univ Cape Town, Dept Mol & Cell Biol, ZA-7701 Rondebosch, South Africa
[3] Biacore Inc, Piscataway, NJ 08854 USA
关键词
D O I
10.1074/jbc.M410203200
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
Histone H2A ubiquitination is a bulky posttranslational modification that occurs at the vicinity of the binding site for linker histones in the nucleosome.Therefore, we took several experimental approaches to investigate the role of ubiquitinated H2A (uH2A) in the binding of linker histones. Our results showed that uH2A was present in situ in histone H1-containing nucleo-cleosomes. Notably in vitro experiments using nucleosomes reconstituted onto 167-bp random sequence and 208-bp (5 S rRNA gene) DNA fragments showed that ubiquitination of H2A did not prevent binding of histone H1 but it rather enhanced the binding of this histone to the nucleosome. We also showed that ubiquitination of H2A did not affect the positioning of the histone octamer in the nucleosome in either the absence or the presence of linker histones.
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页码:4975 / 4982
页数:8
相关论文
共 75 条
[1]   REGULATION OF THE HIGHER-ORDER STRUCTURE OF CHROMATIN BY HISTONES-H1 AND HISTONES-H5 [J].
ALLAN, J ;
COWLING, GJ ;
HARBORNE, N ;
CATTINI, P ;
CRAIGIE, R ;
GOULD, H .
JOURNAL OF CELL BIOLOGY, 1981, 90 (02) :279-288
[2]   THE STRUCTURE OF HISTONE-H1 AND ITS LOCATION IN CHROMATIN [J].
ALLAN, J ;
HARTMAN, PG ;
CRANEROBINSON, C ;
AVILES, FX .
NATURE, 1980, 288 (5792) :675-679
[3]   Linker histone protection of chromatosomes reconstituted on 5S rDNA from Xenopus borealis:: a reinvestigation [J].
An, WJ ;
van Holde, K ;
Zlatanova, J .
NUCLEIC ACIDS RESEARCH, 1998, 26 (17) :4042-4046
[4]   HISTONE HYPERACETYLATION - ITS EFFECTS ON NUCLEOSOME CONFORMATION AND STABILITY [J].
AUSIO, J ;
VANHOLDE, KE .
BIOCHEMISTRY, 1986, 25 (06) :1421-1428
[5]   USE OF SELECTIVELY TRYPSINIZED NUCLEOSOME CORE PARTICLES TO ANALYZE THE ROLE OF THE HISTONE TAILS IN THE STABILIZATION OF THE NUCLEOSOME [J].
AUSIO, J ;
DONG, F ;
VANHOLDE, KE .
JOURNAL OF MOLECULAR BIOLOGY, 1989, 206 (03) :451-463
[6]   Reconstitution of chromatin complexes from high-performance liquid chromatography-purified histones [J].
Ausio, J ;
Moore, SC .
METHODS, 1998, 15 (04) :333-342
[7]  
AUSIO J, 2004, CHROMATIN STRUCTURE, V39, P249
[8]   Histone ubiquitination and chromatin remodeling in mouse spermatogenesis [J].
Baarends, WM ;
Hoogerbrugge, TW ;
Roest, HP ;
Ooms, M ;
Vreeburg, J ;
Hoeijmakers, JHJ ;
Grootegoed, JA .
DEVELOPMENTAL BIOLOGY, 1999, 207 (02) :322-333
[9]  
BALLAL NR, 1975, J BIOL CHEM, V250, P5921
[10]  
BARSOUM J, 1985, J BIOL CHEM, V260, P7688