Codon optimization can improve expression of human genes in Escherichia coli: A multi-gene study.

Journal article

The efficiency of heterologous protein production in Escherichia coli (E. coli) can be diminished by biased codon usage. Approaches normally used to overcome this problem include targeted mutagenesis to remove rare codons or the addition of rare codon tRNAs in specific cell lines. Recently, improvements in technology have enabled cost-effective production of synthetic genes, making this a feasible alternative. To explore this option, the expression patterns in E. coli of 30 human short-chain ...

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Authors: Burgess-Brown, N; Sharma, S; Sobott, F; Loenarz, C; Oppermann, U

• Publication status: Published
• Journal: Protein expression and purification
• Volume: 59
• Issue: 1
• Pages: 94-102
• Publication date: 2008-05-01
• DOI: 10.1016/j.pep.2008.01.008
• EISSN: 1096-0279
• ISSN: 1046-5928
• Language: English
• Keywords: Mass Spectrometry; Gene Expression; Genes, Synthetic; Cloning, Molecular; Recombinant Proteins; Solubility; Electrophoresis, Polyacrylamide Gel; Escherichia coli; Codon; Humans