Issue 4, 2010
From the journal:

Molecular BioSystems

A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli†

Ying Huang,a   William K. Russell,a   Wei Wan,b   Pei-Jing Pai,a   David H. Russella  and  Wenshe Liu*a  

* Corresponding authors

a Department of Chemistry, Texas A&M University, College Station, TX, USA
E-mail: wliu@chem.tamu.edu
Fax: +1 979-845-4719

b Department of Biology, Texas A&M University, College Station, TX, USA

Abstract

By overexpressing the C-terminal domain of the ribosomal protein L11 to decrease release factor 1-mediated termination of protein translation, enhanced amber suppression is achieved in E. coli. This enhanced amber suppression efficiency allows the genetic incorporation of three Nε-acetyl-L-lysines into one GFPUV protein in E. coli.

Graphical abstract: A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli

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Article information

DOI
https://doi.org/10.1039/B920120C
Article type
Communication
Submitted
29 Sep 2009
Accepted
26 Jan 2010
First published
15 Feb 2010

Mol. BioSyst., 2010,6, 683-686

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A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli

Y. Huang, W. K. Russell, W. Wan, P. Pai, D. H. Russell and W. Liu, Mol. BioSyst., 2010, 6, 683 DOI: 10.1039/B920120C

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