Histone H2B ubiquitylation disrupts local and higher-order chromatin compaction

被引：296

作者：

Fierz, Beat ^{[1
]}

Chatterjee, Champak ^{[1
]}

McGinty, Robert K. ^{[1
]}

Bar-Dagan, Maya ^{[1
]}

Raleigh, Daniel P. ^{[2
]}

Muir, Tom W. ^{[1
]}

机构：

[1] Rockefeller Univ, Lab Synthet Prot Chem, New York, NY 10021 USA

[2] SUNY Stony Brook, Dept Chem, Stony Brook, NY 11794 USA

来源：

NATURE CHEMICAL BIOLOGY | 2011年 / 7卷 / 02期

基金：

美国国家卫生研究院; 瑞士国家科学基金会;

关键词：

RNA-POLYMERASE-II; H4-K16; ACETYLATION; GENE-EXPRESSION; HUMAN-CELLS; NUCLEOSOME; FIBER; DYNAMICS; METHYLATION; UBIQUITIN; REVEALS;

D O I：

10.1038/NCHEMBIO.501

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：

Regulation of chromatin structure involves histone posttranslational modifications that can modulate intrinsic properties of the chromatin fiber to change the chromatin state. We used chemically defined nucleosome arrays to demonstrate that H2B ubiquitylation (uH2B), a modification associated with transcription, interferes with chromatin compaction and leads to an open and biochemically accessible fiber conformation. Notably, these effects were specific for ubiquitin, as compaction of chromatin modified with a similar ubiquitin-sized protein, Hub1, was only weakly affected. Applying a fluorescence-based method, we found that uH2B acts through a mechanism distinct from H4 tail acetylation, a modification known to disrupt chromatin folding. Finally, incorporation of both uH2B and acetylated H4 resulted in synergistic inhibition of higher-order chromatin structure formation, possibly a result of their distinct modes of action.

引用

页码：113 / 119

页数：7

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