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H-NS mediated compaction of DNA visualised by atomic force microscopy

机译:H-NS介导的DNA压缩的原子力显微镜观察

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摘要

The Escherichia coli H-NS protein is a nucleoid-associated protein involved in gene regulation and DNA compaction. To get more insight into the mechanism of DNA compaction we applied atomic force microscopy (AFM) to study the structure of H-NS–DNA complexes. On circular DNA molecules two different levels of H-NS induced condensation were observed. H-NS induced lateral condensation of large regions of the plasmid. In addition, large globular structures were identified that incorporated a considerable amount of DNA. The formation of these globular structures appeared not to be dependent on any specific sequence. On the basis of the AFM images, a model for global condensation of the chromosomal DNA by H-NS is proposed.
机译:大肠杆菌H-NS蛋白是一种与核苷相关的蛋白,参与基因调控和DNA压缩。为了更深入地了解DNA压缩的机制,我们应用了原子力显微镜(AFM)来研究H-NS-DNA复合物的结构。在环状DNA分子上,观察到两种不同水平的H-NS诱导的缩合。 H-NS诱导质粒大区域的横向缩合。另外,鉴定出大球状结构并掺入了大量DNA。这些球状结构的形成似乎不依赖于任何特定序列。在原子力显微镜图像的基础上,提出了一种利用H-NS对染色体DNA进行整体缩合的模型。

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