Abstract:
:Biochemical 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.
journal_name
Nat Communjournal_title
Nature communicationsauthors
Pirman NL,Barber KW,Aerni HR,Ma NJ,Haimovich AD,Rogulina S,Isaacs FJ,Rinehart Jdoi
10.1038/ncomms9130subject
Has Abstractpub_date
2015-09-09 00:00:00pages
8130issn
2041-1723pii
ncomms9130journal_volume
6pub_type
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