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

@inproceedings{Roy2011TheTS,
  title={The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine},
  author={Herv{\'e} Roy and Shicong B Zou and Tammy J. Bullwinkle and Benjamin S. Wolfe and Marla S. Gilreath and Craig J Forsyth and William Wiley Navarre and Michael Ibba},
  booktitle={Nature chemical biology},
  year={2011}
}
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… CONTINUE READING
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