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Related Experiment Video

Updated: Mar 28, 2026

Site-Specific Lysine Lactylation via Genetic Code Expansion in E. coli and Mammalian Cells
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Genetic code expansion in stable cell lines enables encoded chromatin modification.

Simon J Elsässer1,2,3, Russell J Ernst1, Olivia S Walker1,2

  • 1Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

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Summary
This summary is machine-generated.

Genetically encoding unnatural amino acids in mammalian cells is now possible with stable genome integration. This allows for homogeneous incorporation and reveals distinct cellular responses to gene expression changes.

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Genetics

Background:

  • Unnatural amino acid incorporation in mammalian cells is typically limited to transient expression, leading to heterogeneous results.
  • This heterogeneity has prevented genome-wide measurements and detailed functional studies.
  • A need exists for methods enabling efficient and homogeneous unnatural amino acid incorporation in stable mammalian cell systems.

Purpose of the Study:

  • To develop a method for stable, genome-wide incorporation of unnatural amino acids in mammalian cells.
  • To investigate the transcriptional responses of different mammalian cell types to amber codon suppression.
  • To explore the functional consequences of genetically encoding post-translational modifications, specifically N-ɛ-acetyl-lysine in histone H3.

Main Methods:

  • Stable integration of the Methanosarcina mazei pyrrolysyl-tRNA synthetase (PylRS)/tRNA(Pyl)CUA pair into the mammalian genome.
  • Utilizing amber codon suppression for homogeneous incorporation of unnatural amino acids into target proteins.
  • Analyzing transcriptional responses in embryonic stem cells and mouse embryonic fibroblasts.
  • Genetically encoding N-ɛ-acetyl-lysine into histone H3 and studying its deposition into chromatin.

Main Results:

  • Demonstrated efficient and homogeneous incorporation of unnatural amino acids into target proteins in diverse mammalian cells via stable genomic integration.
  • Revealed distinct transcriptional responses of embryonic stem cells and mouse embryonic fibroblasts to amber codon suppression.
  • Showcased genetically encoded N-ɛ-acetyl-lysine in histone H3, enabling deposition of pre-acetylated histones via an orthogonal pathway.
  • Determined the consequences of site-specific synthetic lysine acetylation on histone modification sites for gene expression.

Conclusions:

  • Stable genomic integration of the PylRS/tRNA(Pyl)CUA pair enables homogeneous unnatural amino acid incorporation in mammalian cells.
  • This method facilitates genome-wide measurements and the study of protein function.
  • Genetically encoding post-translational modifications like lysine acetylation provides new insights into epigenetic regulation and gene expression.