Document Type
Article
Publication Date
9-12-2011
Abstract
Elongation factor P is modified with (R)‐β‐lysine by the lysyl‐tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate α‐ and β‐lysine recognition by LysRS and PoxA, amino acid replacements were made in the LysRS active site guided by the PoxA structure. A233S LysRS behaved as wild type with α‐lysine, while the G469A and A233S/G469A variants decreased stable α‐lysyl‐adenylate formation. A233S LysRS recognized β‐lysine better than wildtype, suggesting a role for this residue in discriminating α‐ and β‐amino acids. Both enantiomers of β‐lysine were substrates for tRNA aminoacylation by LysRS, which, together with the relaxed specificity of the A233S variant, suggest a possible means to develop systems for in vivo co‐translational insertion of β‐amino acids.
Recommended Citation
Gilreath, M.S., Roy, H., Bullwinkle, T.J., Katz, A., Navarre, W.W. and Ibba M (2011) Beta-lysine discrimination by lysyl-tRNA synthetase. FEBS Letts. 585, 3284-3288. https://doi.org10.1016/j.febslet.2011.09.008
Copyright
Federation of European Biochemical Societies
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 FEBS Letters, volume 585, in 2011 following peer review. The definitive publisher-authenticated version is available online at https://doi.org/10.1016/j.febslet.2011.09.008.