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The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine

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Abstract

The lysyl-tRNA synthetase paralog PoxA modifies elongation factor P (EF-P) with α-lysine at low efficiency. Cell-free extracts containing non–α-lysine substrates of PoxA modified EF-P with a change in mass consistent with addition of β-lysine, a substrate also predicted by genomic analyses. EF-P was efficiently functionally modified with (R)-β-lysine but not (S)-β-lysine or genetically encoded α-amino acids, indicating that PoxA has evolved an activity orthogonal to that of the canonical aminoacyl-tRNA synthetases.

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Figure 1: Amino acid recognition by PoxA.
Figure 2: Modification of EF-P with β-lysine.

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Acknowledgements

We would like to thank Michael Thomas (University of Wisconsin) for the generous gift of (S)-β-lysine. This work was supported by the US National Institutes of Health (GM65183, M.I.), the Canada Institutes for Health Research (MOP-86683 and MSH-87729, W.W.N.) and the Natural Sciences and Engineering Research Council of Canada (RGPIN 386286-10, W.W.N.; Vanier Graduate Scholarship, S.B.Z). We also acknowledge The Ohio State University for partial financial support.

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  1. Hervé Roy

    Present address: Present address: Burnett School of Biomedical Sciences, College of Medicine, University of Central Florida, Orlando, Florida, USA.,

Authors and Affiliations

  1. Department of Microbiology, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA

    Hervé Roy, Tammy J Bullwinkle & Michael Ibba

  2. Department of Molecular Genetics, University of Toronto, Toronto, Ontario, Canada

    S Betty Zou & William W Navarre

  3. Department of Chemistry, Ohio State University, Columbus, Ohio, USA

    Benjamin S Wolfe & Craig J Forsyth

  4. Ohio State Biochemistry Program, Ohio State University, Columbus, Ohio, USA

    Marla S Gilreath & Michael Ibba

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  1. Hervé Roy
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  2. S Betty Zou
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Contributions

H.R., S.B.Z., T.J.B., B.S.W. and M.S.G. performed experiments and analyzed the resulting data; H.R., C.J.F., W.W.N. and M.I. designed experiments and wrote the manuscript.

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Correspondence to Michael Ibba.

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The authors declare no competing financial interests.

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Supplementary Figures 1–5, Supplementary Methods and Supplementary Results (PDF 2199 kb)

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Roy, H., Zou, S., Bullwinkle, T. et al. The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine. Nat Chem Biol 7, 667–669 (2011). https://doi.org/10.1038/nchembio.632

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  • DOI: https://doi.org/10.1038/nchembio.632

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