ArticleNucleic acids research2008
The translation of recombinant proteins in E. coli can be improved by in silico generating and screening random libraries of a -70/+96 mRNA region with respect to the translation initiation codon.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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6 citing papers in PubMed, 19 citations in OpenAlex.
- Snapshots of ADP-ribose bound to Getah virus macro domain reveal an intriguing choreography.Scientific reports · 2020Article
- High-throughput recombinant protein expression in Escherichia coli: current status and future perspectives.Open biology · 2016Review
- Genome engineering for improved recombinant protein expression in Escherichia coli.Microbial cell factories · 2014Review
- Improvement of erythrose reductase activity, deletion of by-products and statistical media optimization for enhanced erythritol production from Yarrowia lipolytica mutant 49.Current microbiology · 2014Article
- Structural basis for antiviral inhibition of the main protease, 3C, from human enterovirus 93.Journal of virology · 2011Article
- The VIZIER project: overview; expectations; and achievements.Antiviral research · 2010Review
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Authors and funding
6 authors at 2 institutions in 1 country.
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Abstract
Recombinant protein translation in Escherichia coli may be limited by stable (i.e. low free energy) secondary structures in the mRNA translation initiation region. To circumvent this issue, we have set-up a computer tool called 'ExEnSo' (Expression Enhancer Software) that generates a random library of 8192 sequences, calculates the free energy of secondary structures of each sequence in the -70/+96 region (base 1 is the translation initiation codon), and then selects the sequence having the highest free energy. The software uses this 'optimized' sequence to create a 5' primer that can be used in PCR experiments to amplify the coding sequence of interest prior to sub-cloning into a prokaryotic expression vector. In this article, we report how ExEnSo was set-up and the results obtained with nine coding sequences with low expression levels in E. coli. The free energy of the -70/+96 region of all these coding sequences was increased compared to the non-optimized sequences. Moreover, the protein expression of eight out of nine of these coding sequences was increased in E. coli, indicating a good correlation between in silico and in vivo results. ExEnSo is available as a free online tool.
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