期刊
EMBO JOURNAL
卷 23, 期 2, 页码 260-271出版社
WILEY
DOI: 10.1038/sj.emboj.7600046
关键词
chromatin remodeling; crystallography; nucleosome structure; protein-DNA interactions
资金
- NIGMS NIH HHS [GM61909, R01 GM061909] Funding Source: Medline
Here we describe 11 crystal structures of nucleosome core particles containing individual point mutations in the structured regions of histones H3 and H4. The mutated residues are located at the two protein - DNA interfaces flanking the nucleosomal dyad. Five of the mutations partially restore the in vivo effects of SWI/SNF inactivation in yeast. We find that even nonconservative mutations of these residues ( which exhibit a distinct phenotype in vivo) have only moderate effects on global nucleosome structure. Rather, local protein - DNA interactions are disrupted and weakened in a subtle and complex manner. The number of lost protein - DNA interactions correlates directly with an increased propensity of the histone octamer to reposition with respect to the DNA, and with an overall destabilization of the nucleosome. Thus, the disruption of only two to six of the similar to120 direct histone - DNA interactions within the nucleosome has a pronounced effect on nucleosome mobility and stability. This has implications for our understanding of how these structures are made accessible to the transcription and replication machinery in vivo.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据