Dual Genetic Encoding of Acetyl-lysine and Non-deacetylatable Thioacetyl-lysine Mediated by Flexizyme

被引：20

作者：

Xiong, Hai ^{[1
]}

Reynolds, Noah M. ^{[1
]}

Fan, Chenguang ^{[1
]}

Englert, Markus ^{[1
]}

Hoyer, Denton ^{[2
]}

Miller, Scott J. ^{[3
]}

Soell, Dieter ^{[1
,3
]}

机构：

[1] Yale Univ, Dept Mol Biophys & Biochem, Whitney Ave 266, New Haven, CT 06511 USA

[2] Yale Univ, Yale Ctr Mol Discovery, West Haven, CT 06516 USA

[3] Yale Univ, Dept Chem, 225 Prospect St, New Haven, CT 06511 USA

来源：

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION | 2016年 / 55卷 / 12期

基金：

美国国家卫生研究院;

关键词：

flexizyme; histone; lysine acetylation; post-translational modifications; thioacetyl-lysine; UNNATURAL AMINO-ACIDS; ESCHERICHIA-COLI; CODE; CHROMATIN; PROTEIN; COMPLEXES; SYSTEM; AMINOACYLATION; INHIBITORS; CROSSTALK;

D O I：

10.1002/anie.201511750

中图分类号：

O6 [化学];

学科分类号：

0703 ;

摘要：

Acetylation of lysine residues is an important post-translational protein modification. Lysine acetylation in histones and its crosstalk with other post-translational modifications in histone and non-histone proteins are crucial to DNA replication, DNA repair, and transcriptional regulation. We incorporated acetyl-lysine (AcK) and the non-hydrolyzable thioacetyl-lysine (ThioAcK) into full-length proteins invitro, mediated by flexizyme. ThioAcK and AcK were site-specifically incorporated at different lysine positions into human histone H3, either individually or in pairs. We demonstrate that the thioacetyl group in histone H3 could not be removed by the histone deacetylase sirtuin type1. This method provides a powerful tool to study protein acetylation and its role in crosstalk between post-translational modifications.

引用

页码：4083 / 4086

页数：4

共 8 条

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