Total chemical synthesis of bivalently modified H3 by improved three-segment native chemical ligation

作     者：Yong Zheng Fangming Wu Shenglong Ling Jia-Bin Li Changlin Tian Yong Zheng;Fangming Wu;Shenglong Ling;Jia-Bin Li;Changlin Tian

作者机构：High Magnetic Field LaboratoryChinese Academy of SciencesHefei 230031China School of Life SciencesUniversity of Science and Technology of ChinaHefei 230027China Jiangsu Key Laboratory of Neuropsychiatric Diseases and College of Pharmaceutical SciencesSoochow UniversitySuzhou 215123China 

出 版 物：《Chinese Chemical Letters》 (中国化学快报（英文版）)

年 卷 期：2020年第31卷第5期

页      面：1267-1270页

核心收录：

学科分类：081704[工学-应用化学] 07[理学] 08[工学] 0817[工学-化学工程与技术] 070303[理学-有机化学] 0703[理学-化学] 

基　　金：supported by the National Natural Science Foundation of China(Nos.21708036,31470740,U1732161) Anhui Provincial Natural Science Foundation (No.1808085QC63) 

主　　题：Chemical protein synthesis Native chemical ligation Histone H3 Methylation Acetylation Nucleosome core particles 

摘      要：The H3 bivalent modifications of trimethylationat Lys9 and acetylation at Lys18(H3-K9 Me3-K18 Ac) were identified to collectively recruit TRIM33 in the nodal signaling *** understand the underlying mechanism of TRIM33 recruitment,the nucleosome core particles(NCPs) containing full-length H3-K9 Me3-K18 Ac were indispensable *** we developed a pseudo dipeptide strategy to efficiently prepare peptide segments,facilitating the chemical synthesis of H3-K9 Me3-K18 Ac at a tens of milligram *** synthetic H3-K9 Me3-K18 Ac was then examined by CD spectroscopy,which demonstrated a prominent shift compared to recombinant ***,bivalently modified NCPs were assembled and verified by gel mobility shift assay with good homogeneity.