Addicting diverse bacteria to a noncanonical amino acid (original) (raw)

Nature Chemical Biology volume 12, pages 138–140 (2016)Cite this article

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Abstract

Engineered orthogonal translation systems have greatly enabled the expansion of the genetic code using noncanonical amino acids (NCAAs). However, the impact of NCAAs on organismal evolution remains unclear, in part because it is difficult to force the adoption of new genetic codes in organisms. By reengineering TEM-1 β-lactamase to be dependent on a NCAA, we maintained bacterial NCAA dependence for hundreds of generations without escape.

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Figure 1: Characterization of NCAA dependent β-lactamase variants.

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Figure 2: β-lactamase variant TEM-1.B9 maintained NCAA dependence in different bacterial species during serial culture.

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NCBI Reference Sequence

Protein Data Bank

References

  1. Wong, J.T. Proc. Natl. Acad. Sci. USA 80, 6303–6306 (1983).
    Article CAS Google Scholar
  2. Rovner, A.J. et al. Nature 518, 89–93 (2015).
    Article CAS Google Scholar
  3. Mandell, D.J. et al. Nature 518, 55–60 (2015).
    Article CAS Google Scholar
  4. Lemeignan, B., Sonigo, P. & Marlière, P. J. Mol. Biol. 231, 161–166 (1993).
    Article CAS Google Scholar
  5. Chin, J.W. et al. J. Am. Chem. Soc. 124, 9026–9027 (2002).
    Article CAS Google Scholar
  6. Wang, J., Xie, J. & Schultz, P.G. J. Am. Chem. Soc. 128, 8738–8739 (2006).
    Article CAS Google Scholar
  7. Xie, J., Supekova, L. & Schultz, P.G. ACS Chem. Biol. 2, 474–478 (2007).
    Article CAS Google Scholar
  8. Liu, C.C. & Schultz, P.G. Annu. Rev. Biochem. 79, 413–444 (2010).
    Article CAS Google Scholar
  9. Hammerling, M.J. et al. Nat. Chem. Biol. 10, 178–180 (2014).
    Article CAS Google Scholar
  10. Bacher, J.M., Bull, J.J. & Ellington, A.D. BMC Evol. Biol. 3, 24 (2003).
    Article Google Scholar
  11. Bacher, J.M. & Ellington, A.D. J. Bacteriol. 183, 5414–5425 (2001).
    Article CAS Google Scholar
  12. Wang, Q. et al. ChemBioChem 15, 1744–1749 (2014).
    Article CAS Google Scholar
  13. Kato, Y. PeerJ 3, e1247 (2015).
    Article Google Scholar
  14. Cooley, R.B. et al. Biochemistry 53, 1916–1924 (2014).
    Article CAS Google Scholar
  15. Sakamoto, K. et al. Structure 17, 335–344 (2009).
    Article CAS Google Scholar
  16. Ohtake, K. et al. Sci. Rep. 5, 9762 (2015).
    Article CAS Google Scholar
  17. Bradford, P.A. Clin. Microbiol. Rev. 14, 933–951 (2001).
    Article CAS Google Scholar
  18. Fonzé, E. et al. Acta Crystallogr. D Biol. Crystallogr. 51, 682–694 (1995).
    Article Google Scholar
  19. Baba, T. et al. Mol. Syst. Biol. 2, 2006.0008 (2006).
    Article Google Scholar
  20. Lajoie, M.J. et al. Science 342, 357–360 (2013).
    Article CAS Google Scholar
  21. Thyer, R., Robotham, S.A., Brodbelt, J.S. & Ellington, A.D. J. Am. Chem. Soc. 137, 46–49 (2015).
    Article CAS Google Scholar
  22. Gibson, D.G. et al. Nat. Methods 6, 343–345 (2009).
    Article CAS Google Scholar
  23. Hashimoto-Gotoh, T. et al. Gene 241, 185–191 (2000).
    Article CAS Google Scholar
  24. Chung, C.T., Niemela, S.L. & Miller, R.H. Proc. Natl. Acad. Sci. USA 86, 2172–2175 (1989).
    Article CAS Google Scholar
  25. Stec, B., Holtz, K.M., Wojciechowski, C.L. & Kantrowitz, E.R. Acta Crystallogr. D Biol. Crystallogr. 61, 1072–1079 (2005).
    Article Google Scholar
  26. Labute, P. Proteins 75, 187–205 (2009).
    Article CAS Google Scholar
  27. Labute, P. J. Chem. Inf. Model. 50, 792–800 (2010).
    Article CAS Google Scholar
  28. Clark, A.M. & Labute, P. J. Chem. Inf. Model. 47, 1933–1944 (2007).
    Article CAS Google Scholar

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Acknowledgements

This work was supported by the following grants: National Security Science and Engineering Faculty Fellowship grant FA9550-10-1-0169 to A.D.E. Welch Foundation grant F-1654. Defense Advanced Research Projects Agency N66001-14-2-4051 to A.D.E. Air Force Office of Scientific Research grant FA9550-14-1-0089 to A.D.E. Defense Advanced Research Projects Agency HR0011-15-C0095 to A.D.E.

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Authors and Affiliations

  1. Center for Systems and Synthetic Biology, University of Texas at Austin, Austin, Texas, USA
    Drew S Tack, Jared W Ellefson, Ross Thyer, Bo Wang, Jimmy Gollihar, Matthew T Forster & Andrew D Ellington

Authors

  1. Drew S Tack
  2. Jared W Ellefson
  3. Ross Thyer
  4. Bo Wang
  5. Jimmy Gollihar
  6. Matthew T Forster
  7. Andrew D Ellington

Contributions

D.S.T. designed and performed experiments and wrote the manuscript. J.W.E. designed experiments and wrote the manuscript. R.T. designed experiments and wrote the manuscript. B.W. screened TEM-1 variants. M.T.F. screened TEM-1 variants. J.G. performed computational analysis using the Molecular Operating Environment. A.D.E. directed experimental work and wrote the manuscript.

Corresponding author

Correspondence toAndrew D Ellington.

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The authors declare no competing financial interests.

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Tack, D., Ellefson, J., Thyer, R. et al. Addicting diverse bacteria to a noncanonical amino acid.Nat Chem Biol 12, 138–140 (2016). https://doi.org/10.1038/nchembio.2002

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