Document Type
Article
Publication Date
8-14-2011
Abstract
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.
Recommended Citation
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
Copyright
Nature Publishing Group
Included in
Amino Acids, Peptides, and Proteins Commons, Biochemistry Commons, Cellular and Molecular Physiology Commons, Molecular Biology Commons, Nucleic Acids, Nucleotides, and Nucleosides Commons, Other Biochemistry, Biophysics, and Structural Biology Commons
Comments
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/
A free-to-read copy of the final published article is available here.