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Glycine to glutamic acid misincorporation observed in a recombinant protein expressed by Escherichia coli cells
Authors:Huang Yunping  O'Mara Brian  Conover Matthew  Ludwig Richard  Fu Jinmei  Tao Li  Li Zheng Jian  Rieble Siegfried  Grace Michael J  Russell Reb J
Institution:Department of Biologics Product & Process Development, Bristol-Myers Squibb Technical Operations, Princeton, New Jersey 08543, USA. yunping.huang@bms.com
Abstract:A novel amino acid misincorporation, in which the intended glycine (Gly) residues were replaced by a glutamic acid (Glu), was observed in a recombinant protein expressed by Escherichia coli. The misincorporation was identified by peptide mapping and liquid chromatography-tandem mass spectrometric analysis on proteolyzed peptides of the protein and verified using the corresponding synthetic peptides containing the misincorporated residues. Analysis of the distribution of the misincorporated residues and their codon usage shows strong correlation between this misincorporation and the use of rarely used codon within the E. coli expression system. Results in this study suggest that the usage of the rare codon GGA has resulted in a Glu for Gly misincorporation.
Keywords:glycine to glutamic acid misincorporation  recombinant  Escherichia coli  rare codon  GGA
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