The majority of proteins in eukaryote cells are subjected to amino-terminal acetylation. This co-translational modification can affect the stability of a protein and also regulate its biological function. Amino-terminally acetylated recombinant proteins cannot be produced using prokaryote expression systems, such as E. coli , as these cells lack the appropriate N-α-terminal acetyltransferase complexes. Here we describe a simple protocol that allows the recombinant expression and purification of NatB-dependent amino-terminally acetylated proteins from E. coli . © Springer Science+Business Media, LLC 2013.
CITATION STYLE
Johnson, M., Geeves, M. A., & Mulvihill, D. P. (2013). Production of amino-terminally acetylated recombinant proteins in E. coli. Methods in Molecular Biology, 981, 193–200. https://doi.org/10.1007/978-1-62703-305-3_15
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