Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends.

Crenarchaeal chromatin proteins Cren7 and Sul7 compact DNA by inducing rigid bends.
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DOI:
10.1093/nar/gks1053
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发表时间:
2013-01-07
影响因子:
14.9
通讯作者:
Dame RT
Dame RT
中科院分区:
生物学2区
文献类型:
--
作者:
Driessen RP;Meng H;Suresh G;Shahapure R;Lanzani G;Priyakumar UD;White MF;Schiessel H;van Noort J;Dame RT

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古细菌的染色质蛋白与细菌和真核生物的染色质蛋白具有分子和功能上的相似性。这些蛋白质在将基因组DNA组织成紧密的类核中起着重要的作用。Cren7和Sul7是两个古细菌核相关蛋白,它们在结构上同源,但在序列水平上不保守。共晶结构表明,这两种蛋白质在与DNA结合时产生了急剧的弯曲。在这项研究中,我们利用原子力显微镜、分子动力学模拟和磁镊子研究了这些蛋白质的结构特性。我们证明了Cren7和Sul7都以相似的程度压缩DNA分子。使用理论模型,我们量化了结合到DNA上的单个蛋白质的数量作为蛋白质浓度的函数,并表明高达3.5 pN的力不会影响这种结合。此外,我们研究了Cren7和Sul7诱导的弯曲角的灵活性,并表明蛋白质- dna复合物的灵活性不同于类似的细菌和真核生物dna弯曲蛋白。
Archaeal chromatin proteins share molecular and functional similarities with both bacterial and eukaryotic chromatin proteins. These proteins play an important role in functionally organizing the genomic DNA into a compact nucleoid. Cren7 and Sul7 are two crenarchaeal nucleoid-associated proteins, which are structurally homologous, but not conserved at the sequence level. Co-crystal structures have shown that these two proteins induce a sharp bend on binding to DNA. In this study, we have investigated the architectural properties of these proteins using atomic force microscopy, molecular dynamics simulations and magnetic tweezers. We demonstrate that Cren7 and Sul7 both compact DNA molecules to a similar extent. Using a theoretical model, we quantify the number of individual proteins bound to the DNA as a function of protein concentration and show that forces up to 3.5 pN do not affect this binding. Moreover, we investigate the flexibility of the bending angle induced by Cren7 and Sul7 and show that the protein–DNA complexes differ in flexibility from analogous bacterial and eukaryotic DNA-bending proteins.
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