Electrostatic effect of H1-histone protein binding on nucleosome repeat length
Electrostatic effect of H1-histone protein binding on nucleosome repeat length
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DOI：
10.1088/1478-3975/11/4/044001
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发表时间：
2014-08-01
期刊：
影响因子：
2
通讯作者：
Teif, Vladimir B.
中科院分区：
文献类型：
--
作者：
Cherstvy, Andrey G.;Teif, Vladimir B.
在一个简单的生物物理模型中，我们描述了H1组蛋白的静电结合对染色质中核小体重复长度的影响。包裹DNA的长度优化了其与组蛋白核心的结合能和DNA包裹的弹性能损失。从我们的模型中预测的影响程度与核小体重复长度随H1/核小体比率的线性变化的系统实验数据一致（Woodcock C L et al . 2006 Chromos）。Res. 14 17-25)。我们将我们的模型与不同细胞类型和生物体的数据进行比较，每个核小体结合H1组蛋白的比例差异很大。我们强调这种非特异性组蛋白- dna电荷平衡机制在调节核小体的定位和真核细胞中染色质纤维的压实程度方面的重要性。
Within a simple biophysical model we describe the effect of electrostatic binding of H1 histone proteins on the nucleosome repeat length in chromatin. The length of wrapped DNA optimizes its binding energy to the histone core and the elastic energy penalty of DNA wrapping. The magnitude of the effect predicted from our model is in agreement with the systematic experimental data on the linear variation of nucleosome repeat lengths with H1/nucleosome ratio (Woodcock C L et al 2006 Chromos. Res. 14 17-25). We compare our model to the data for different cell types and organisms, with a widely varying ratio of bound H1 histones per nucleosome. We underline the importance of this non-specific histone-DNA charge-balance mechanism in regulating the positioning of nucleosomes and the degree of compaction of chromatin fibers in eukaryotic cells.