Journal
FEBS LETTERS
Volume 586, Issue 20, Pages 3716-3722Publisher
WILEY
DOI: 10.1016/j.febslet.2012.08.031
Keywords
Synthetic biology; Phosphoserine; Phosphoproteomics; Genetic code; Genetic code expansion; Genome engineering
Funding
- National Institute of General Medical Sciences
- National Science Foundation
- DARPA CLIO [N66001-12C-4020]
- NIDDK [K01DK089006]
- Deutsche Forschungsgemeinschaft [HE5802/1-1]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0950474] Funding Source: National Science Foundation
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Genetically encoded phosphoserine incorporation programmed by the UAG codon was achieved by addition of engineered elongation factor and an archaeal aminoacyl-tRNA synthetase to the normal Escherichia coli translation machinery (Park et al., 2011) Science 333, 1151) [2]. However, protein yield suffers from expression of the orthogonal phosphoserine translation system and competition with release factor 1 (RF-1). In a strain lacking RF-1, phosphoserine phosphatase, and where seven UAG codons residing in essential genes were converted to UAA, phosphoserine incorporation into GFP and WNK4 was significantly elevated, but with an accompanying loss in cellular fitness and viability. (c) 2012 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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