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Nature Research, Nature Communications, 1(6), 2015

DOI: 10.1038/ncomms9130

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A flexible codon in genomically recoded Escherichia coli permits programmable protein phosphorylation

Journal article published in 2015 by Natasha L. Pirman, Karl W. Barber ORCID, Hans R. Aerni, Natalie J. Ma, Adrian D. Haimovich ORCID, Svetlana Rogulina, Farren J. Isaacs, Jesse Rinehart
This paper is made freely available by the publisher.
This paper is made freely available by the publisher.

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Abstract

AbstractBiochemical investigation of protein phosphorylation events is limited by inefficient production of the phosphorylated and non-phosphorylated forms of full-length proteins. Here using a genomically recoded strain of E. coli with a flexible UAG codon we produce site-specific serine- or phosphoserine-containing proteins, with purities approaching 90%, from a single recombinant DNA. Specifically, we synthesize human MEK1 kinase with two serines or two phosphoserines, from one DNA template, and demonstrate programmable kinase activity. Programmable protein phosphorylation is poised to help reveal the structural and functional information encoded in the phosphoproteome.