Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System

Lysine acetylation is a reversible post-translational modification (PTM) vastly employed in many biological events, including regulating gene expression and dynamic transitions in chromatin remodeling. We have developed the first one-pot bio-orthogonal flexizyme system in which both acetyl-lysine (A...

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Detalles Bibliográficos
Autores principales: Xiao, Qiuyun, Liu, Zihan, Zhao, Xuan, Xiong, Hai
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Frontiers Media S.A. 2020
Materias:
Bioengineering and Biotechnology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7010957/
https://www.ncbi.nlm.nih.gov/pubmed/32117920
http://dx.doi.org/10.3389/fbioe.2020.00037
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author Xiao, Qiuyun
Liu, Zihan
Zhao, Xuan
Xiong, Hai
author_facet Xiao, Qiuyun
Liu, Zihan
Zhao, Xuan
Xiong, Hai
author_sort Xiao, Qiuyun
collection PubMed
description Lysine acetylation is a reversible post-translational modification (PTM) vastly employed in many biological events, including regulating gene expression and dynamic transitions in chromatin remodeling. We have developed the first one-pot bio-orthogonal flexizyme system in which both acetyl-lysine (AcK) and non-hydrolysable thioacetyl-lysine (ThioAcK) were site-specifically incorporated into human histone H3 and H4 at different lysine positions in vitro, either individually or in pairs. In addition, the high accuracy of this system moving toward one-pot synthesis of desired histone variants is also reported.
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spelling pubmed-70109572020-02-28 Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System Xiao, Qiuyun Liu, Zihan Zhao, Xuan Xiong, Hai Front Bioeng Biotechnol Bioengineering and Biotechnology Lysine acetylation is a reversible post-translational modification (PTM) vastly employed in many biological events, including regulating gene expression and dynamic transitions in chromatin remodeling. We have developed the first one-pot bio-orthogonal flexizyme system in which both acetyl-lysine (AcK) and non-hydrolysable thioacetyl-lysine (ThioAcK) were site-specifically incorporated into human histone H3 and H4 at different lysine positions in vitro, either individually or in pairs. In addition, the high accuracy of this system moving toward one-pot synthesis of desired histone variants is also reported. Frontiers Media S.A. 2020-02-04 /pmc/articles/PMC7010957/ /pubmed/32117920 http://dx.doi.org/10.3389/fbioe.2020.00037 Text en Copyright © 2020 Xiao, Liu, Zhao and Xiong. http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
spellingShingle Bioengineering and Biotechnology
Xiao, Qiuyun
Liu, Zihan
Zhao, Xuan
Xiong, Hai
Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title_full Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title_fullStr Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title_full_unstemmed Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title_short Multiple Site-Specific One-Pot Synthesis of Two Proteins by the Bio-Orthogonal Flexizyme System
title_sort multiple site-specific one-pot synthesis of two proteins by the bio-orthogonal flexizyme system
topic Bioengineering and Biotechnology
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7010957/
https://www.ncbi.nlm.nih.gov/pubmed/32117920
http://dx.doi.org/10.3389/fbioe.2020.00037
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