Suppr超能文献

结合分子动力学模拟和评分方法,对染色质体中的泛素化连接组蛋白进行计算建模。

Combining molecular dynamics simulations and scoring method to computationally model ubiquitylated linker histones in chromatosomes.

机构信息

Department of Chemistry, University of Konstanz, Konstanz, Germany.

Theory Department, Max-Planck Institute for Polymer Research, Mainz, Germany.

出版信息

PLoS Comput Biol. 2023 Aug 1;19(8):e1010531. doi: 10.1371/journal.pcbi.1010531. eCollection 2023 Aug.

Abstract

The chromatin in eukaryotic cells plays a fundamental role in all processes during a cell's life cycle. This nucleoprotein is normally tightly packed but needs to be unpacked for expression and division. The linker histones are critical for such packaging processes and while most experimental and simulation works recognize their crucial importance, the focus is nearly always set on the nucleosome as the basic chromatin building block. Linker histones can undergo several modifications, but only few studies on their ubiquitylation have been conducted. Mono-ubiquitylated linker histones (HUb), while poorly understood, are expected to influence DNA compaction. The size of ubiquitin and the globular domain of the linker histone are comparable and one would expect an increased disorder upon ubiquitylation of the linker histone. However, the formation of higher order chromatin is not hindered and ubiquitylation of the linker histone may even promote gene expression. Structural data on chromatosomes is rare and HUb has never been modeled in a chromatosome so far. Descriptions of the chromatin complex with HUb would greatly benefit from computational structural data. In this study we generate molecular dynamics simulation data for six differently linked HUb variants with the help of a sampling scheme tailored to drive the exploration of phase space. We identify conformational sub-states of the six HUb variants using the sketch-map algorithm for dimensionality reduction and iterative HDBSCAN for clustering on the excessively sampled, shallow free energy landscapes. We present a highly efficient geometric scoring method to identify sub-states of HUb that fit into the nucleosome. We predict HUb conformations inside a nucleosome using on-dyad and off-dyad chromatosome structures as reference and show that unbiased simulations of HUb produce significantly more fitting than non-fitting HUb conformations. A tetranucleosome array is used to show that ubiquitylation can even occur in chromatin without too much steric clashes.

摘要

真核细胞中的染色质在细胞生命周期中的所有过程中都起着基本作用。这种核蛋白通常紧密包装,但为了表达和分裂需要解包。连接组蛋白对于这种包装过程至关重要,虽然大多数实验和模拟工作都认识到它们的重要性,但重点几乎总是放在核小体作为基本染色质构建块上。连接组蛋白可以经历几种修饰,但只有少数关于它们泛素化的研究。单泛素化连接组蛋白(HUb)虽然了解甚少,但预计会影响 DNA 压缩。泛素的大小和连接组蛋白的球形结构域相当,人们预计连接组蛋白泛素化会增加无序性。然而,更高阶染色质的形成并没有受阻,连接组蛋白的泛素化甚至可能促进基因表达。关于染色质体的结构数据很少,而且迄今为止,HUb 从未在染色质体中建模。带有 HUb 的染色质复合物的描述将极大地受益于计算结构数据。在这项研究中,我们在一个专门设计的采样方案的帮助下,为六种不同连接的 HUb 变体生成分子动力学模拟数据,以驱动对相空间的探索。我们使用草图映射算法识别六个 HUb 变体的构象亚态,用于降维和迭代 HDBSCAN 聚类过度采样的浅层自由能景观。我们提出了一种高效的几何评分方法,用于识别适合核小体的 HUb 亚态。我们使用在二联体和非二联体染色质体结构作为参考的方法来预测核小体内部的 HUb 构象,并表明无偏模拟的 HUb 产生的拟合构象明显多于不拟合的 HUb 构象。使用四联体核小体阵列来表明,即使在没有太多空间位阻的情况下,染色质也可以发生泛素化。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/8ed5/10442151/18ef197bc3b5/pcbi.1010531.g001.jpg

文献AI研究员

20分钟写一篇综述,助力文献阅读效率提升50倍。

立即体验

用中文搜PubMed

大模型驱动的PubMed中文搜索引擎

马上搜索

文档翻译

学术文献翻译模型,支持多种主流文档格式。

立即体验