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Lys34 of translation elongation factor EF-P is hydroxylated by YfcM

Nature Chemical Biology volume 8, pages 695697 (2012) | Download Citation

Abstract

Lys34 of the conserved translation elongation factor P (EF-P) is post-translationally lysinylated by YjeK and YjeA—a modification that is critical for bacterial virulence. Here we show that the currently accepted Escherichia coli EF-P modification pathway is incomplete and lacks a final hydroxylation step mediated by YfcM, an enzyme distinct from deoxyhypusine hydroxylase that catalyzes the final maturation step of eukaryotic initiation factor 5A, the eukaryotic EF-P homolog.

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Acknowledgements

We thank N. Morrice and J. Rappsilber for invaluable help and advice on amino acid analyses and L. Arike and T. Tammsalu for help with MS analyses. This research was supported by grants from the Deutsche Forschungsgemeinschaft WI3285/1-1, the Human Frontiers of Science Foundation (RGY88/2008), the European Molecular Biology Organization young investigator program (to D.N.W.) and the Estonian Science Foundation grant no. 9289 (to J.R.). L.P. and G.C.A. are supported by the European Social Fund program Mobilitas grants MJD144 and MJD99, respectively. MS analyses were, in part, supported by the European Regional Development Fund through the Center of Excellence in Chemical Biology (Institute of Technology, University of Tartu).

Author information

Author notes

    • Lauri Peil

    Present address: Wellcome Trust Centre for Cell Biology, University of Edinburgh, Edinburgh, UK.

    • Lauri Peil
    •  & Agata L Starosta

    These authors contributed equally to this work.

Affiliations

  1. Institute of Technology, University of Tartu, Tartu, Estonia.

    • Lauri Peil
    • , Gemma C Atkinson
    •  & Tanel Tenson
  2. Gene Center and Department for Biochemistry, Center for integrated Protein Science Munich, University of Munich, Munich, Germany.

    • Agata L Starosta
    •  & Daniel N Wilson
  3. Institute of Molecular and Cell Biology, University of Tartu, Tartu, Estonia.

    • Kai Virumäe
    •  & Jaanus Remme

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Contributions

L.P., A.L.S., J.R. and D.N.W. designed research; L.P. performed and analyzed MS data, A.L.S. and K.V. performed biochemistry; G.C.A. performed bioinformatics; and L.P., A.L.S., T.T., J.R. and D.N.W. analyzed data and wrote the paper.

Competing interests

The authors declare no competing financial interests.

Corresponding authors

Correspondence to Jaanus Remme or Daniel N Wilson.

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DOI

https://doi.org/10.1038/nchembio.1001

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