Title
Β-Lysine Discrimination By Lysyl-Trna Synthetase
Keywords
β-Amino acid; Aminoacyl-tRNA synthetase; Lysine; Translation; tRNA
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. © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
Publication Date
10-20-2011
Publication Title
FEBS Letters
Volume
585
Issue
20
Number of Pages
3284-3288
Document Type
Article
Personal Identifier
scopus
DOI Link
https://doi.org/10.1016/j.febslet.2011.09.008
Copyright Status
Unknown
Socpus ID
80054080054 (Scopus)
Source API URL
https://api.elsevier.com/content/abstract/scopus_id/80054080054
STARS Citation
Gilreath, Marla S.; Roy, Hervé; Bullwinkle, Tammy J.; Katz, Assaf; and Navarre, William W., "Β-Lysine Discrimination By Lysyl-Trna Synthetase" (2011). Scopus Export 2010-2014. 2985.
https://stars.library.ucf.edu/scopus2010/2985