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

Hervé Roy, S Betty Zou, Tammy J Bullwinkle, Benjamin S Wolfe, Marla S Gilreath, Craig J Forsyth, William W Navarre, Michael Ibba

Department of Microbiology, Center for RNA Biology, Ohio State University, Columbus, Ohio, USA.

Nature chemical biology 2011 Oct

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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.

Citation

Hervé Roy, S Betty Zou, Tammy J Bullwinkle, Benjamin S Wolfe, Marla S Gilreath, Craig J Forsyth, William W Navarre, Michael Ibba. The tRNA synthetase paralog PoxA modifies elongation factor-P with (R)-β-lysine. Nature chemical biology. 2011 Oct;7(10):667-9