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

Ying Huang, William Russell, Wei Wan, Pei Jing Pai, David H. Russell, Wenshe Liu

Research output: Contribution to journalArticle

45 Citations (Scopus)

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.

Original languageEnglish (US)
Pages (from-to)683-686
Number of pages4
JournalMolecular BioSystems
Volume6
Issue number4
DOIs
StatePublished - 2010
Externally publishedYes

Fingerprint

Amber
Escherichia coli Proteins
Translational Peptide Chain Termination
Amino Acids
Lysine
Escherichia coli
ribosomal protein L11

ASJC Scopus subject areas

  • Biotechnology
  • Molecular Biology

Cite this

A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli. / Huang, Ying; Russell, William; Wan, Wei; Pai, Pei Jing; Russell, David H.; Liu, Wenshe.

In: Molecular BioSystems, Vol. 6, No. 4, 2010, p. 683-686.

Research output: Contribution to journalArticle

Huang, Ying ; Russell, William ; Wan, Wei ; Pai, Pei Jing ; Russell, David H. ; Liu, Wenshe. / A convenient method for genetic incorporation of multiple noncanonical amino acids into one protein in Escherichia coli. In: Molecular BioSystems. 2010 ; Vol. 6, No. 4. pp. 683-686.
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