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

Nature Communications

Volumn 6, Issue , 2015, Pages

  Pirman, Natasha L ^a,b   Barber, Karl W ^a,b   Aerni, Hans R ^a,b   Ma, Natalie J ^b   Haimovich, Adrian D ^b   Rogulina, Svetlana ^a,b   Isaacs, Farren J ^b   Rinehart, Jesse ^a,b  

^a YALE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b YALE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ALKALINE PHOSPHATASE; BETA LACTAMASE; GREEN FLUORESCENT PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE KINASE 1; PHOSPHOSERINE; SERINE; TRANSFER RNA; MAP2K1 PROTEIN, HUMAN; STOP CODON;

BACTERIUM; BIOCHEMICAL COMPOSITION; ENZYME ACTIVITY; GENOMICS; PROTEIN;

AMINO ACID METABOLISM; ARTICLE; CODON; CONTROLLED STUDY; DNA TEMPLATE; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE DOSAGE; MASS SPECTROMETRY; NONHUMAN; NORTHERN BLOTTING; PROTEIN PHOSPHORYLATION; PROTEIN STABILITY; BACTERIAL GENOME; BIOSYNTHESIS; GENETICS; HUMAN; METABOLISM; PHOSPHORYLATION; STOP CODON; TRANSGENIC ORGANISM;

ESCHERICHIA COLI;

CODON, TERMINATOR; ESCHERICHIA COLI; GENOME, BACTERIAL; GREEN FLUORESCENT PROTEINS; HUMANS; MAP KINASE KINASE 1; ORGANISMS, GENETICALLY MODIFIED; PHOSPHORYLATION; PHOSPHOSERINE; SERINE;

EID: 84941298014     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms9130     Document Type: Article

References (25)

1. Olsen, J. V. & Mann, M. Status of large-scale analysis of post-translational modifications by mass spectrometry. Mol. Cell. Proteomics. 12, 3444-3452 (2013).
2. Hornbeck, P. V. et al. PhosphoSitePlus: a comprehensive resource for investigating the structure and function of experimentally determined post-translational modifications in man and mouse. Nucleic Acids Res. 40, D261-D270 (2012).
3. Mok, J. et al. Deciphering protein kinase specificity through large-scale analysis of yeast phosphorylation site motifs. Sci. Signal 3, ra12 (2010).
4. Park, H. S. et al. Expanding the genetic code of Escherichia coli with phosphoserine. Science 333, 1151-1154 (2011).
5. Isaacs, F. J. et al. Precise manipulation of chromosomes in vivo enables genome-wide codon replacement. Science 333, 348-353 (2011).
6. Heinemann, I. U. et al. Enhanced phosphoserine insertion during Escherichia coli protein synthesis via partial UAG codon reassignment and release factor 1 deletion. FEBS Lett. 586, 3716-3722 (2012).
7. Aerni, H. R., Shifman, M. A., Rogulina, S., O'Donoghue, P. & Rinehart, J. Revealing the amino acid composition of proteins within an expanded genetic code. Nucleic Acids Res. 43, e8 (2014).
8. Lajoie, M. J. et al. Genomically recoded organisms expand biological functions. Science 342, 357-360 (2013).
9. Kinoshita, E., Kinoshita-Kikuta, E., Takiyama, K. & Koike, T. Phosphate-binding tag, a new tool to visualize phosphorylated proteins. Mol. Cell. Proteomics 5, 749-757 (2006).
10. Takeya, K., Loutzenhiser, K., Shiraishi, M., Loutzenhiser, R. & Walsh, M. P. A highly sensitive technique to measure myosin regulatory light chain phosphorylation: the first quantification in renal arterioles. Am. J. Physiol. Renal Physiol. 294, F1487-F1492 (2008).
11. Yamada, S. et al. Separation of a phosphorylated histidine protein using phosphate affinity polyacrylamide gel electrophoresis. Anal. Biochem. 360, 160-162 (2007).
12. Kinoshita-Kikuta, E., Aoki, Y., Kinoshita, E. & Koike, T. Label-free kinase profiling using phosphate affinity polyacrylamide gel electrophoresis. Mol. Cell. Proteomics 6, 356-366 (2007).
13. Lee, S. et al. A facile strategy for selective incorporation of phosphoserine into histones. Angew. Chem. Int. Ed. 52, 5771-5775 (2013).
14. Eggertsson, G. & Soll, D. Transfer ribonucleic acid-mediated suppression of termination codons in Escherichia coli. Microbiol. Rev. 52, 354-374 (1988).
15. Demeshkina, N., Jenner, L., Westhof, E., Yusupov, M. & Yusupova, G. A new understanding of the decoding principle on the ribosome. Nature 484, 256-259 (2012).
16. Steege, D. A. A nucleotide change in the anticodon of an Escherichia coli serine transfer RNA results in supD-amber suppression. Nucleic Acids Res. 11, 3823-3832 (1983).
17. Normanly, J., Ogden, R. C., Horvath, S. J. & Abelson, J. Changing the identity of a transfer RNA. Nature 321, 213-219 (1986).
18. Scholl, F. A., Dumesic, P. A. & Khavari, P. A. Effects of active MEK1 expression in vivo. Cancer Lett. 230, 1-5 (2005).
19. Zheng, C. F. & Guan, K. L. Activation of MEK family kinases requires phosphorylation of two conserved Ser/Thr residues. EMBO J. 13, 1123-1131 (1994).
20. Alessi, D. R. et al. Mechanism of activation of protein kinase B by insulin and IGF-1. EMBO J. 15, 6541-6551 (1996).
21. Kyriakis, J. M., Brautigan, D. L., Ingebritsen, T. S. & Avruch, J. pp54 microtubule-associated protein-2 kinase requires both tyrosine and serine/threonine phosphorylation for activity. J. Biol. Chem. 266, 10043-10046 (1991).
22. Raingeaud, J. et al. Pro-inflammatory cytokines and environmental stress cause p38 mitogen-activated protein kinase activation by dual phosphorylation on tyrosine and threonine. J. Biol. Chem. 270, 7420-7426 (1995).
23. Sawyer, N. et al. Designed phosphoprotein recognition in Escherichia coli. ACS Chem. Biol. 9, 2502-2507 (2014).
24. Davis, L. & Chin, J. W. Designer proteins: applications of genetic code expansion in cell biology. Nat. Rev. Mol. Cell Biol. 13, 168-182 (2012).
25. Oza, J. et al. Robust production of recombinant phosphoproteins using cell-free protein synthesis. Nat. Commun 6, 8168 (2015).