Use of Serine/Threonine Ligation for the Total Chemical Synthesis of HMGA1a Protein with Site-Specific Lysine Acetylations

被引：5
|
作者：
Liu, Heng [1 ]
Liu, Han [1 ]
Li, Xuechen [1 ]
机构：
[1] Univ Hong Kong, Dept Chem, State Key Lab Synthet Chem, Pokfulam Rd, Hong Kong, Peoples R China
来源：
CHEMPLUSCHEM | 2019年 / 84卷 / 07期
基金：
美国国家科学基金会;
关键词：
acetylation; HMG proteins; kinase assays; post-translational modifications; Ser; Thr ligation; TEIXOBACTIN ANALOGS; SER/THR LIGATION; PHOSPHORYLATION; IDENTIFICATION; SERINE; SUBSTITUTION; DAPTOMYCIN; APOPTOSIS; PEPTIDES; GROWTH;
D O I：
10.1002/cplu.201900130
中图分类号：
O6 [化学];
学科分类号：
0703 ;
摘要：
High-mobility-group (HMG) proteins are a class of abundant non-histone nuclear proteins, among which HMGA1a is well-known for its association with transcription regulation as well as tumor formation and disease development. To study the functions of post-translational modifications, homogeneous HMGA1a protein with site-specific lysine acetylations (64/66/70/73) has been chemically synthesized. The full-length HMGA1a protein was assembled through two Ser/Thr ligations of three peptide fragments at Gly37-Thr37 and Thr75-Thr76 sites, respectively. Further in vitro studies with chemically synthesized proteins suggested that these acetylations did not significantly affect the CK2-catalyzed phosphorylation on the HMGA1a acidic tail.
引用
收藏
页码：779 / 785
页数：7
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