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ß-Lysine discrimination by lysyl-tRNA synthetase

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  • Marla S Gilreath
  • Hervé Roy
  • Tammy J Bullwinkle
  • Assaf Katz
  • William W Navarre
  • Michael Ibba
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.
OriginalsprogEngelsk
TidsskriftF E B S Letters
Vol/bind585
Udgave nummer20
Sider (fra-til)3284-8
Antal sider5
ISSN0014-5793
DOI
StatusUdgivet - 2011

ID: 38488882