Probing the Effect of Ubiquitinated Histone H2A on mono-nucleosomes by Translocation Dynamics Study through Solid-state Nanopores
Probing the Effect of Ubiquitinated Histone H2A on mono-nucleosomes by Translocation Dynamics Study through Solid-state Nanopores
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DOI：
10.1021/acs.nanolett.1c02978
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发表时间：
2022
期刊：
影响因子：
--
通讯作者：
Qing Zhao
中科院分区：
文献类型：
--
作者：
Rui Hu;Cuifang Liu;Wenlong Lu;Guangha Wei;Dapeng Yu;Wei Li;Ping Chen;Guohong Li;Qing Zhao
Post-translational modifications (PTMs), such as ubiquitination, are critically important in regulating genetic expressions by adjusting the nucleosome stability. A fast and label-free technology inspecting dynamic nucleosome structures can facilitate the interrogation of PTMs effects. Here we leverage the advantages of mechanically stable solid-state nanopores and detect the effect of a ubiquitinated histone on mononucleosomes at the single-molecule level. By comparing the translocation dynamics of natural and cross-linked mononucleosomes, we verified that the nucleosomal DNA unravelled from histones in natural mononucleosomes. Furthermore, we found that a turning point of voltage corresponds to the onset of nucleosome rupture. More importantly, we reveal that ubH2A stabilizes the nucleosome by shifting the turning point to a larger value and investigated the effect of ubiquitination on different histones (ubH2A and ubH2B). These findings open promising possibilities for developing a miniaturized and portable device for the fast screening of PTMs on nucleosomes.
