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Atomic force microscopy of chromatin arrays reveal non-monotonic salt dependence of array compaction in solution

机译:染色质阵列的原子力显微镜显示溶液中阵列压缩的非单调盐依赖性

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摘要

Compaction of DNA in chromatin is a hallmark of the eukaryotic cell and unravelling its structure is required for an understanding of DNA involving processes. Despite strong experimental efforts, many questions concerning the DNA packing are open. In particular, it is heavily debated whether an ordered structure referred to as the “30 nm fibre” exist in vivo. Scanning probe microscopy has become a cutting edge technology for the high-resolution imaging of DNA- protein complexes. Here, we perform high-resolution atomic force microscopy of non-cross-linked chromatin arrays in liquid, under different salt conditions. A statistical analysis of the data reveals that array compaction is salt dependent in a non-monotonic fashion. A simple physical model can qualitatively explain the observed findings due to the opposing effects of salt dependent stiffening of DNA, nucleosome stability and histone-histone interactions. While for different salt concentrations different compaction states are observed, our data do not provide support for the existence of regular chromatin fibres. Our studies add new insights into chromatin structure, and with that contribute to a further understanding of the DNA condensation.
机译:染色质中DNA的紧缩是真核细胞的标志,要弄清涉及过程的DNA,需要弄清其结构。尽管作出了巨大的实验努力,但有关DNA包装的许多问题仍未解决。特别是,在体内是否存在一种被称为“ 30 nm光纤”的有序结构,引起了激烈的争论。扫描探针显微镜已成为对DNA-蛋白质复合物进行高分辨率成像的尖端技术。在这里,我们在不同的盐分条件下,对液体中的非交联染色质阵列进行高分辨率原子力显微镜观察。数据的统计分析表明,阵列压实以非单调方式依赖于盐。一个简单的物理模型可以定性地解释观察到的发现,这是由于盐依赖的DNA硬化,核小体稳定性和组蛋白-组蛋白相互作用的相反作用。虽然对于不同的盐浓度观察到不同的压实状态,但我们的数据不能为规则染色质纤维的存在提供支持。我们的研究为染色质结构增加了新的见解,并有助于进一步了解DNA缩合。

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