ß-Lysine discrimination by lysyl-tRNA synthetase
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Elongation factor P is modified with (R)-ß-lysine by the lysyl-tRNA synthetase (LysRS) paralog PoxA. PoxA specificity is orthogonal to LysRS, despite their high similarity. To investigate a- and ß-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 a-lysine, while the G469A and A233S/G469A variants decreased stable a-lysyl-adenylate formation. A233S LysRS recognized ß-lysine better than wildtype, suggesting a role for this residue in discriminating a- and ß-amino acids. Both enantiomers of ß-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 ß-amino acids.
Originalsprog | Engelsk |
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Tidsskrift | F E B S Letters |
Vol/bind | 585 |
Udgave nummer | 20 |
Sider (fra-til) | 3284-8 |
Antal sider | 5 |
ISSN | 0014-5793 |
DOI | |
Status | Udgivet - 2011 |
ID: 38488882