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.
Roy, H., Zou, S.B., Bullwinkle, T.J., Wolfe, B.S., Gilreath, M.S., Forsyth, C.J., Navarre, W.W. and Ibba, M. (2011) The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine. Nature Chem. Biol. 7, 667-669. https://doi.org10.1038/nchembio.632
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This is a pre-copy-editing, author-produced PDF of an article accepted for publication in Nature Chemical Biology, volume 7, in 2011 following peer review. The final publication may differ and is available at Springer via https://doi.org/10.1038/nchembio.632/
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