The convergent chemical synthesis of histone H3 protein for site-specific acetylation at Lys56 and ubiquitination at Lys122

被引：27
作者：
Qi, Yun-Kun [1 ,2 ]
He, Qiao-Qiao [1 ]
Ai, Hua-Song [1 ]
Guo, Jing [1 ]
Li, Jia-Bin [1 ,2 ]
机构：
[1] Tsinghua Univ, Tsinghua Peking Ctr Life Sci, Dept Chem, Beijing 100084, Peoples R China
[2] Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Peoples R China
来源：
CHEMICAL COMMUNICATIONS | 2017年 / 53卷 / 29期
关键词：
PEPTIDE HYDRAZIDES; CHAPERONE RTT106; STRUCTURAL BASIS; LIGATION; H2B; UBIQUITYLATION; METHYLATION; CYSTEINE; DEUBIQUITINASES; NUCLEOSOMES;
D O I：
10.1039/c7cc01721a
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
Deposition of (H3-H4)(2) tetramers is believed to be the critical step in nucleosome assembly. Site-specific acetylation and ubiquitination of histone H3 have been speculated to synergistically facilitate the formation and deposition of (H3-H4)(2) tetramers. Here we report our endeavors toward the first chemical synthesis of homogenous histone H3, which bears Lys56 acetylation and Lys122 ubiquitination, for in vitro biochemical and biophysical studies.
引用
收藏
页码：4148 / 4151
页数：4
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