Targeted amino-terminal acetylation of recombinant proteins in E. coli

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Abstract

One major limitation in the expression of eukaryotic proteins in bacteria is an inability to post-translationally modify the expressed protein. Amino-terminal acetylation is one such modification that can be essential for protein function. By co-expressing the fission yeast NatB complex with the target protein in E.coli, we report a simple and widely applicable method for the expression and purification of functional N-terminally acetylated eukaryotic proteins.

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Johnson, M., Coulton, A. T., Geeves, M. A., & Mulvihill, D. P. (2010). Targeted amino-terminal acetylation of recombinant proteins in E. coli. PLoS ONE, 5(12). https://doi.org/10.1371/journal.pone.0015801

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