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

By Matthew Johnson, Arthur T. Couton, Michael A. Geeves and Daniel P. Mulvihill

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

Topics: QH301, QH426, QR
Year: 2010
OAI identifier: oai:kar.kent.ac.uk:26186

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