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

2011; Nature Portfolio; Volume: 7; Issue: 10 Linguagem: Inglês

10.1038/nchembio.632

1552-4469

Hervé Roy, Shengwei Zou, Tammy J. Bullwinkle, Benjamin Scott Wolfe, Marla S. Gilreath, Craig J. Forsyth, William Wiley Navarre, Michael Ibba,

Bacterial Genetics and Biotechnology

PoxA is a lysyl-tRNA synthetase paralog that post-translationally modifies elongation factor P (EF-P) with a lysine moiety. Further biochemical analysis reveals that (R)-β-lysine, rather than the more abundant α-amino acid, is the preferred substrate for PoxA. 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.