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FEBS Lett. 2012 Oct 19;586(20):3716-22. doi: 10.1016/j.febslet.2012.08.031. Epub 2012 Sep 13.

Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion.

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1
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06520-8144, USA.

Abstract

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). 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.

PMID:
22982858
PMCID:
PMC3473164
DOI:
10.1016/j.febslet.2012.08.031
[Indexed for MEDLINE]
Free PMC Article
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