Histone tails and the H3 αN helix regulate nucleosome mobility and stability

被引:117
作者
Ferreira, Helder [1 ]
Somers, Joanna [1 ]
Webster, Ryan [1 ]
Flaus, Andrew [1 ]
Owen-Hughes, Tom [1 ]
机构
[1] Univ Dundee, Wellcome Trust Bioctr, Dept Biochem, Div Gene Regulat & Express, Dundee DD1 5EH, Scotland
基金
英国惠康基金;
关键词
D O I
10.1128/MCB.02229-06
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
Nucleosomes fulfill the apparently conflicting roles of compacting DNA within eukaryotic genomes while permitting access to regulatory factors. Central to this is their ability to stably associate with DNA while retaining the ability to undergo rearrangements that increase access to the underlying DNA. Here, we have studied different aspects of nucleosome dynamics including nucleosome sliding, histone dimer exchange, and DNA wrapping within nucleosomes. We find that alterations to histone proteins, especially the histone tails and vicinity of the histone H3 alpha N helix, can affect these processes differently, suggesting that they are mechanistically distinct. This raises the possibility that modifications to histone proteins may provide a means of fine-tuning specific aspects of the dynamic properties of nucleosomes to the context in which they are located.
引用
收藏
页码:4037 / 4048
页数:12
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