Discovery and Investigation of Natural Editing Function against Artificial Amino Acids in Protein Translation.

ABSTRACT: Fluorine being not substantially present in the chemistry of living beings is an attractive element in tailoring novel chemical, biophysical, and pharmacokinetic properties of peptides and proteins. The hallmark of ribosome-mediated artificial amino acid incorporation into peptides and proteins is a broad substrate tolerance, which is assumed to rely on the absence of evolutionary pressure for efficient editing of artificial amino acids. We used the well-characterized editing proficient isoleucyl-tRNA synthetase (IleRS) from Escherichia coli to investigate the crosstalk of aminoacylation and editing activities against fluorinated amino acids. We show that translation of trifluoroethylglycine (TfeGly) into proteins is prevented by hydrolysis of TfeGly-tRNA^Ile in the IleRS

SUBMITTER: Voller JS 

PROVIDER: S-EPMC5269655 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature