期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 8, 页码 4922-4933出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku150
关键词
-
资金
- American Heart Association [0815460D, 10PRE3150036]
- OSUCCC
- James Pelotonia Fellowship
- American Cancer Society [IRG-6700344]
- National Institutes of Health (NIH) [GM083055]
- Career Award in the Basic Biomedical Sciences from the Burroughs Wellcome Fund
- National Science Foundation [MCB0845695]
- Human Frontier Science Program [RGY0057/2009]
- NIH [R01GM083055]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [0845695] Funding Source: National Science Foundation
Nucleosomes contain similar to 146 bp of DNA wrapped around a histone protein octamer that controls DNA accessibility to transcription and repair complexes. Posttranslational modification (PTM) of histone proteins regulates nucleosome function. To date, only modest changes in nucleosome structure have been directly attributed to histone PTMs. Histone residue H3(T118) is located near the nucleosome dyad and can be phosphorylated. This PTM destabilizes nucleosomes and is implicated in the regulation of transcription and repair. Here, we report gel electrophoretic mobility, sucrose gradient sedimentation, thermal disassembly, micrococcal nuclease digestion and atomic force microscopy measurements of two DNA-histone complexes that are structurally distinct from nucleosomes. We find that H3(T118ph) facilitates the formation of a nucleosome duplex with two DNA molecules wrapped around two histone octamers, and an altosome complex that contains one DNA molecule wrapped around two histone octamers. The nucleosome duplex complex forms within short similar to 150 bp DNA molecules, whereas altosomes require at least similar to 250 bp of DNA and form repeatedly along 3000 bp DNA molecules. These results are the first report of a histone PTM significantly altering the nucleosome structure.
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