Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition

Thiirane linkers directed histone H2A diubiquitination suggests plasticity in 53BP1 recognition

Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted in vitro binding studie...

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Veröffentlicht in:Chemical communications (Cambridge, England) England), 2019-10, Vol.55 (84), p.12639-12642
Hauptverfasser: Liang, Jun, Gong, Qingyue, Li, Ying, Zheng, Yong, Zheng, Ji-Shen, Tian, Changlin, Li, Jia-Bin
Format: Artikel
Sprache:eng
Schlagworte:
Histones
Histones - chemistry
Organic chemistry
Plastic properties
Polyubiquitin - chemistry
Protein Binding
Recognition
Recombinant Proteins - chemistry
Sulfides - chemistry
Tumor Suppressor p53-Binding Protein 1 - chemistry
Ubiquitination
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Beschreibung
Zusammenfassung:Polyubiquitination with diverse linkages on histones provides another layer of accuracy and complexity for epigenetic regulation, which is rarely studied. Herein, K27 or K48-diubiquitin modified H2A analogues were chemically synthesized using thiirane linkers. These permitted in vitro binding studies suggested the plasticity of ubiquitin chains in 53BP1 recognition. Four diubiquitinated H2A analogues were newly synthesized and used to reveal the plasticity of ubiquitin chains in 53BP1 recognition.
ISSN:1359-7345
1364-548X
DOI:10.1039/c9cc05526f