Histone H2A Ubiquitination Reinforces Mechanical Stability and Asymmetry at the Single-Nucleosome Level
Monoubiquitination at lysine 119 of histone H2A (ubH2A) is a prevalent post-translational modification that is associated with gene repression in the context of chromatin. However, the direct function of ubH2A on nucleosome is poorly understood. Here we identified the effect of ubH2A on nucleosome using single-molecule magnetic tweezers. We revealed that ubH2A stabilizes the nucleosome by blocking the peeling of DNA from the histone octamer. Each ubH2A reinforces one-half of the outer wrap and introduces a robust asymmetry for nucleosome unfolding. Furthermore, a real-time deubiquitination process confirmed that ubH2A-nucleosome is sequentially deubiquitinated and restored to the unmodified nucleosome state. These results provide a novel mechanism to understand the repression of the passage of RNA or DNA polymerases through the ubH2A-nucleosome barrier during gene transcription or replication.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2020 |
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| Erschienen: |
2020 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:142 |
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| Enthalten in: |
Journal of the American Chemical Society - 142(2020), 7 vom: 19. Feb., Seite 3340-3345 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Xiao, Xue [VerfasserIn] |
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| Links: |
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| Themen: |
9007-49-2 |
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| Anmerkungen: |
Date Completed 09.11.2020 Date Revised 09.11.2020 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1021/jacs.9b12448 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| PPN (Katalog-ID): |
NLM305996592 |
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| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Monoubiquitination at lysine 119 of histone H2A (ubH2A) is a prevalent post-translational modification that is associated with gene repression in the context of chromatin. However, the direct function of ubH2A on nucleosome is poorly understood. Here we identified the effect of ubH2A on nucleosome using single-molecule magnetic tweezers. We revealed that ubH2A stabilizes the nucleosome by blocking the peeling of DNA from the histone octamer. Each ubH2A reinforces one-half of the outer wrap and introduces a robust asymmetry for nucleosome unfolding. Furthermore, a real-time deubiquitination process confirmed that ubH2A-nucleosome is sequentially deubiquitinated and restored to the unmodified nucleosome state. These results provide a novel mechanism to understand the repression of the passage of RNA or DNA polymerases through the ubH2A-nucleosome barrier during gene transcription or replication | ||
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| 700 | 1 | |a Liu, Cuifang |e verfasserin |4 aut | |
| 700 | 1 | |a Pei, Yingxin |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Yi-Zhou |e verfasserin |4 aut | |
| 700 | 1 | |a Kong, Jingwei |e verfasserin |4 aut | |
| 700 | 1 | |a Lu, Ke |e verfasserin |4 aut | |
| 700 | 1 | |a Ma, Lu |e verfasserin |4 aut | |
| 700 | 1 | |a Dou, Shuo-Xing |e verfasserin |4 aut | |
| 700 | 1 | |a Wang, Peng-Ye |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Guohong |e verfasserin |4 aut | |
| 700 | 1 | |a Chen, Ping |e verfasserin |4 aut | |
| 700 | 1 | |a Li, Wei |e verfasserin |4 aut | |
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