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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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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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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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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