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

Socpus ID

80054080054 (Scopus)

Source API URL

https://api.elsevier.com/content/abstract/scopus_id/80054080054

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