Abstract |
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.
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Authors | Rui Hu, Cuifang Liu, Wenlong Lu, Guanghao Wei, Dapeng Yu, Wei Li, Ping Chen, Guohong Li, Qing Zhao |
Journal | Nano letters
(Nano Lett)
Vol. 22
Issue 3
Pg. 888-895
(02 09 2022)
ISSN: 1530-6992 [Electronic] United States |
PMID | 35060726
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
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Topics |
- Histones
(chemistry, genetics, metabolism)
- Nanopores
- Nucleosomes
(metabolism)
- Protein Processing, Post-Translational
- Ubiquitination
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