Suppr超能文献

阐明核小体间相互作用及组蛋白尾部的作用。

Elucidating internucleosome interactions and the roles of histone tails.

机构信息

Department of Physics, George Washington University, Washington, DC, USA.

出版信息

Biophys J. 2013 Jul 2;105(1):194-9. doi: 10.1016/j.bpj.2013.05.021.

Abstract

The nucleosome is the first level of genome organization and regulation in eukaryotes where negatively charged DNA is wrapped around largely positively charged histone proteins. Interaction between nucleosomes is dominated by electrostatics at long range and guided by specific contacts at short range, particularly involving their flexible histone tails. We have thus quantified how internucleosome interactions are modulated by salts (KCl, MgCl2) and histone tail deletions (H3, H4 N-terminal), using small-angle x-ray scattering and theoretical modeling. We found that measured effective charges at low salts are ∼1/5th of the theoretically predicted renormalized charges and that H4 tail deletion suppresses the attraction at high salts to a larger extent than H3 tail deletion.

摘要

核小体是真核生物基因组组织和调控的第一个层次,带负电荷的 DNA 缠绕在带大量正电荷的组蛋白上。核小体之间的相互作用主要受长程静电作用控制,并由短程特定接触引导,特别是涉及它们的柔性组蛋白尾巴。因此,我们使用小角度 X 射线散射和理论建模来量化盐(KCl、MgCl2)和组蛋白尾巴缺失(H3、H4 N 端)如何调节核小体之间的相互作用。我们发现,在低盐条件下测量到的有效电荷约为理论预测的重归一化电荷的 1/5,并且 H4 尾巴缺失比 H3 尾巴缺失更能抑制高盐下的吸引力。

相似文献

引用本文的文献

3
Histone Tail Conformations: A Fuzzy Affair with DNA.组蛋白尾部构象:与 DNA 的模糊关系。
Trends Biochem Sci. 2021 Jul;46(7):564-578. doi: 10.1016/j.tibs.2020.12.012. Epub 2021 Feb 4.
7
Revealing transient structures of nucleosomes as DNA unwinds.随着DNA解旋揭示核小体的瞬时结构。
Nucleic Acids Res. 2014 Jul;42(13):8767-76. doi: 10.1093/nar/gku562. Epub 2014 Jul 2.

本文引用的文献

1
Modelling chromatin structure and dynamics: status and prospects.建模染色质结构和动力学:现状与展望。
Curr Opin Struct Biol. 2012 Apr;22(2):151-9. doi: 10.1016/j.sbi.2012.01.006. Epub 2012 Feb 2.

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