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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