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FEBS Lett. 2011 Oct 20;585(20):3284-8. doi: 10.1016/j.febslet.2011.09.008. Epub 2011 Sep 12.

β-Lysine discrimination by lysyl-tRNA synthetase.

Author information

1
Ohio State Biochemistry Program, Center for RNA Biology, Ohio State University, Columbus, OH 43210, USA.

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.

PMID:
21925499
PMCID:
PMC3196068
DOI:
10.1016/j.febslet.2011.09.008
[Indexed for MEDLINE]
Free PMC Article

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