...
首页> 外文期刊>Ultramicroscopy >Removal of histone tails from nucleosome dissects the physical mechanisms of salt-induced aggregation, linker histone H1-induced compaction, and 30-nm fiber formation of the nucleosome array
【24h】

Removal of histone tails from nucleosome dissects the physical mechanisms of salt-induced aggregation, linker histone H1-induced compaction, and 30-nm fiber formation of the nucleosome array

机译:从核小体上去除组蛋白尾巴解剖了盐诱导的聚集,接头组蛋白H1诱导的紧实以及核小体阵列的30 nm纤维形成的物理机制。

获取原文
获取原文并翻译 | 示例
           

摘要

In order to reveal the roles of histone tails in the formation of higher-order chromatin structures, we employed atomic force microscopy (AFM), and an in vitro reconstitution system to examine the properties of reconstituted chromatin composed of tail-less histones and a long DNA (106-kb plasmid) template. The tail-less nucleosomes did not aggregate at high salt concentrations or with an excess amount of core histones, in contrast with the behavior of nucleosomal arrays composed of nucleosomes containing normal, N-terminal tails. Analysis of our nucleosome distributions reveals that the attractive interaction between tailless nucleosomes is weakened. Addition of linker histone H1 into the tail-less nucleosomal array failed to promote the formation of 30 nm chromatin fibers that are usually formed in the normal nucleosomal array. These results demonstrate that the attractive interaction between nucleosomes via histone tails plays a critical role in the formation of the uniform 30-nm chromatin fiber.
机译:为了揭示组蛋白尾巴在高级染色质结构形成中的作用,我们采用原子力显微镜(AFM)和体外重构系统来检查由无尾组蛋白和长尾巴组成的重构染色质的特性。 DNA(106-kb质粒)模板。与由含有正常N末端尾巴的核小体组成的核小体阵列的行为相反,无尾核小体在高盐浓度或核心组蛋白过量时不会聚集。对我们的核小体分布的分析表明,无尾核小体之间的吸引力相互作用减弱了。将接头组蛋白H1添加到无尾核小体阵列中无法促进通常在正常核小体阵列中形成的30 nm染色质纤维的形成。这些结果表明,核糖体之间通过组蛋白尾部的有吸引力的相互作用在均匀的30 nm染色质纤维的形成中起关键作用。

著录项

相似文献

  • 外文文献
获取原文

客服邮箱:kefu@zhangqiaokeyan.com

京公网安备:11010802029741号 ICP备案号:京ICP备15016152号-6 六维联合信息科技 (北京) 有限公司©版权所有
  • 客服微信

  • 服务号