Pyrrolysyl-tRNA synthetase variants reveal ancestral aminoacylation function

FEBS Lett. 2013 Oct 1;587(19):3243-8. doi: 10.1016/j.febslet.2013.08.018. Epub 2013 Aug 28.

Abstract

Pyrrolysyl-tRNA synthetase (PylRS) is a class IIc aminoacyl-tRNA synthetase that is related to phenylalanyl-tRNA synthetase (PheRS). Genetic selection provided PylRS variants with a broad range of specificity for diverse non-canonical amino acids (ncAAs). One variant is a specific phenylalanine-incorporating enzyme. Structural models of the PylRSamino acid complex show that the small pocket size and π-interaction play an important role in specific recognition of Phe and the engineered PylRS active site resembles that of Escherichia coli PheRS.

Keywords: Non-canonical amino acid; Phenylalanyl-tRNA synthetase; Pyrrolysyl-tRNA synthetase; Superfolder green fluorescent protein.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.

MeSH terms

  • Amino Acyl-tRNA Synthetases / chemistry
  • Amino Acyl-tRNA Synthetases / genetics
  • Amino Acyl-tRNA Synthetases / metabolism*
  • Aminoacylation
  • Codon
  • Escherichia coli / enzymology
  • Evolution, Molecular
  • Lysine / analogs & derivatives*
  • Lysine / metabolism
  • Mutation
  • Substrate Specificity

Substances

  • Codon
  • Amino Acyl-tRNA Synthetases
  • pyrrolysine
  • Lysine