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

Natasha L. Pirman, Karl W. Barber, Hans R. Aerni, Natalie J. Ma, Adrian D. Haimovich, Svetlana Rogulina, Farren J. Isaacs and Jesse Rinehart ()
Additional contact information
Natasha L. Pirman: Yale University
Karl W. Barber: Yale University
Hans R. Aerni: Yale University
Natalie J. Ma: Cellular and Developmental Biology, Yale University
Adrian D. Haimovich: Cellular and Developmental Biology, Yale University
Svetlana Rogulina: Yale University
Farren J. Isaacs: Cellular and Developmental Biology, Yale University
Jesse Rinehart: Yale University

Nature Communications, 2015, vol. 6, issue 1, 1-6

Abstract: 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.

Date: 2015
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms9130 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms9130

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms9130

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().