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Related Experiment Video

Updated: Jul 10, 2026

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Site Specific Lysine Acetylation of Histones for Nucleosome Reconstitution using Genetic Code Expansion in Escherichia coli

Published on: December 26, 2020

Adding pyrrolysine to the Escherichia coli genetic code.

Olivier Namy¹, Yu Zhou, Sarath Gundllapalli

¹Institut de Genetique et Microbiologie, Université Paris-Sud, CNRS UMR8621, Orsay F-91405, France.

|October 31, 2007

Summary

The Pyl insertion structure (PYLIS) does not affect pyrrolysine (Pyl) or Cyc incorporation in E. coli. However, d-ornithine significantly enhances Pyl insertion, revealing it as a direct precursor.

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Area of Science:

Biochemistry
Molecular Biology
Genetics

Background:

Pyrrolysyl-tRNA synthetase and tRNA(Pyl) enable pyrrolysine (Pyl) insertion at UAG codons.
An RNA hairpin, Pyl insertion structure (PYLIS), enhances Pyl insertion in archaea.

Purpose of the Study:

To investigate the impact of PYLIS on Pyl and Cyc incorporation in Escherichia coli.
To identify precursors for pyrrolysine biosynthesis in an E. coli system.

Main Methods:

Utilized a quantitative lacZ-luc tandem reporter system in E. coli.
Assessed Pyl and Cyc incorporation levels with and without PYLIS.
Tested the effect of exogenous d-ornithine supply on suppression efficiency.

Main Results:

PYLIS presence did not alter the levels of Pyl or Cyc incorporation.
Exogenous d-ornithine significantly increased pyrrolysine suppression efficiency.
d-ornithine was identified as a direct precursor to pyrrolysine.

Conclusions:

PYLIS does not enhance pyrrolysine incorporation in the E. coli system.
d-ornithine is a direct precursor for pyrrolysine synthesis in E. coli, impacting suppression efficiency.