Skip to main content

Thank you for visiting nature.com. You are using a browser version with limited support for CSS. To obtain the best experience, we recommend you use a more up to date browser (or turn off compatibility mode in Internet Explorer). In the meantime, to ensure continued support, we are displaying the site without styles and JavaScript.

  • News & Views
  • Published:

Easing selenocysteine into proteins

Selenocysteinyl-tRNASec is used by many organisms from all three domains of life to incorporate selenocysteine (Sec) site-specifically into certain proteins. Two recent reports have identified a new Sec synthase that catalyzes the last step in the generation of this aminoacyl-tRNA in eukarya and archaea.

This is a preview of subscription content, access via your institution

Access options

Buy this article

Prices may be subject to local taxes which are calculated during checkout

Figure 1: Selenocysteine can be incorporated into specific proteins via read-through of an internal, in-frame UGA codon.
Figure 2: The biosynthesis of Sec-tRNASec in bacteria (top pathway) and in archaea and eukarya (bottom pathway).

References

  1. Bock, A. et al. Mol. Microbiol. 5, 515–520 (1991).

    Article  CAS  Google Scholar 

  2. Boyington, J.C., Gladyshev, V.N., Khangulov, S.V., Stadtman, T.C. & Sun, P.D. Science 275, 1305–1308 (1997).

    Article  CAS  Google Scholar 

  3. Raaijmakers, H.C. & Romao, M.J. J. Biol. Inorg. Chem. 11, 849–854 (2006).

    Article  CAS  Google Scholar 

  4. Bock, A., Thanbichler, M., Rother, M. & Resch, A. in Aminoacyl-tRNA Synthetases (eds. Ibba, M., Francklyn, C.S. & Cusack, S.) 320–327 (Landes Biosciences, Georgetown, Texas, USA, 2005).

    Google Scholar 

  5. Xu, X.M. et al. PLoS Biol. 5, e4 (2006).

    Article  Google Scholar 

  6. Yuan, J. et al. Proc. Natl. Acad. Sci. USA 103, 18923–18927 (2006).

    Article  CAS  Google Scholar 

  7. Leinfelder, W., Zehelein, E., Mandrand-Berthelot, M.A. & Bock, A. Nature 331, 723–725 (1988).

    Article  CAS  Google Scholar 

  8. Forchhammer, K., Leinfelder, W., Boesmiller, K., Veprek, B. & Bock, A. J. Biol. Chem. 266, 6318–6323 (1991).

    CAS  PubMed  Google Scholar 

  9. Bilokapic, S., Korencic, D., Soll, D. & Weygand-Durasevic, I. Eur. J. Biochem. 271, 694–702 (2004).

    Article  CAS  Google Scholar 

  10. Wu, X.Q. & Gross, H.J. Nucleic Acids Res. 21, 5589–5594 (1993).

    Article  CAS  Google Scholar 

  11. Kaiser, J.T. et al. Biochemistry 44, 13315–13327 (2005).

    Article  CAS  Google Scholar 

  12. Carlson, B.A. et al. Proc. Natl. Acad. Sci. USA 101, 12848–12853 (2004).

    Article  CAS  Google Scholar 

  13. Sauerwald, A. et al. Science 307, 1969–1972 (2005).

    Article  CAS  Google Scholar 

  14. Gelpi, C., Sontheimer, E.J. & Rodriguez-Sanchez, J.L. Proc. Natl. Acad. Sci. USA 89, 9739–9743 (1992).

    Article  CAS  Google Scholar 

  15. Kernebeck, T., Lohse, A.W. & Grotzinger, J. Hepatology 34, 230–233 (2001).

    Article  CAS  Google Scholar 

  16. Leinfelder, W., Forchhammer, K., Veprek, B., Zehelein, E. & Bock, A. Proc. Natl. Acad. Sci. USA 87, 543–547 (1990).

    Article  CAS  Google Scholar 

  17. Forchhammer, K. & Bock, A. J. Biol. Chem. 266, 6324–6328 (1991).

    CAS  PubMed  Google Scholar 

  18. Feng, L. et al. in Aminoacyl-tRNA Synthetases (eds. Ibba, M., Francklyn, C.S. & Cusack, S.) 314–319 (Landes Biosciences, Georgetown, Texas, USA, 2005).

    Google Scholar 

  19. Krzycki, J.A. Curr. Opin. Microbiol. 8, 706–712 (2005).

    Article  CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Ethics declarations

Competing interests

The author declares no competing financial interests.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Hendrickson, T. Easing selenocysteine into proteins. Nat Struct Mol Biol 14, 100–101 (2007). https://doi.org/10.1038/nsmb0207-100

Download citation

  • Issue Date:

  • DOI: https://doi.org/10.1038/nsmb0207-100

This article is cited by

Search

Quick links

Nature Briefing

Sign up for the Nature Briefing newsletter — what matters in science, free to your inbox daily.

Get the most important science stories of the day, free in your inbox. Sign up for Nature Briefing