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Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli
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Genetically encoding ε-N-benzoyllysine in proteins.

Yanli Ji1, Conghui Ren, Hui Miao

  • 1State Key Laboratory and Institute of Elemento-Organic Chemistry, College of Chemistry, Nankai University, Tianjin 300071, China. wxuan@nankai.edu.cn.

Chemical Communications (Cambridge, England)
|January 21, 2021
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Summary

We genetically encoded benzoyl-lysine (BzK) into proteins, enabling histone modification and sirtuin debenzoylase activity analysis. This new method advances the study of post-translational modifications.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Epigenetics

Background:

  • Lysine benzoylation is a recently identified post-translational modification (PTM).
  • Histone modifications play crucial roles in gene regulation.
  • Understanding PTMs requires tools for their specific incorporation and analysis.

Purpose of the Study:

  • To genetically encode ε-N-benzoyl-lysine (BzK) into recombinant proteins.
  • To apply BzK incorporation for histone modification.
  • To enable the analysis of sirtuin debenzoylase activity.

Main Methods:

  • Genetic encoding of BzK in *E. coli* and mammalian cells.
  • Site-specific incorporation of BzK into proteins.
  • Modification of histone proteins with BzK.
  • Assay development for sirtuin debenzoylase activity.

Main Results:

  • Successful genetic encoding and incorporation of BzK in both bacterial and mammalian systems.
  • Demonstrated BzK modification of histone proteins.
  • Established a method to analyze sirtuin debenzoylase activity on BzK-modified histones.

Conclusions:

  • Genetic encoding of BzK provides a powerful tool for studying lysine benzoylation.
  • This methodology facilitates research into histone modifications and epigenetic regulation.
  • The developed system is applicable for analyzing enzymes involved in debenzoylation.