Unknown

Dataset Information

0

Ribosomal incorporation of backbone modified amino acids via an editing-deficient aminoacyl-tRNA synthetase.

ABSTRACT: The ability to incorporate non-canonical amino acids (ncAA) using translation offers researchers the ability to extend the functionality of proteins and peptides for many applications including synthetic biology, biophysical and structural studies, and discovery of novel ligands. Here we describe the high promiscuity of an editing-deficient valine-tRNA synthetase (ValRS T222P). Using this enzyme, we demonstrate ribosomal translation of 11 ncAAs including those with novel side chains, ?,?-disubstitutions, and cyclic ?-amino acids.

SUBMITTER: Iqbal ES 

PROVIDER: S-EPMC5993425 | biostudies-literature | 2018 Feb

REPOSITORIES: biostudies-literature

Json Xml
altmetric image

Publications

Ribosomal incorporation of backbone modified amino acids via an editing-deficient aminoacyl-tRNA synthetase.

Iqbal Emil S ES   Dods Kara K KK   Hartman Matthew C T MCT  

Organic & biomolecular chemistry 20180201 7

The ability to incorporate non-canonical amino acids (ncAA) using translation offers researchers the ability to extend the functionality of proteins and peptides for many applications including synthetic biology, biophysical and structural studies, and discovery of novel ligands. Here we describe the high promiscuity of an editing-deficient valine-tRNA synthetase (ValRS T222P). Using this enzyme, we demonstrate ribosomal translation of 11 ncAAs including those with novel side chains, α,α-disubst  ...[more]

Similar Datasets

Unknown Steric and thermodynamic limits of design for the incorporation of large unnatural amino acids in aminoacyl-tRNA synthetase enzymes.
| S-EPMC4442682 | biostudies-literature
Unknown Incorporation of fluorotyrosines into ribonucleotide reductase using an evolved, polyspecific aminoacyl-tRNA synthetase.
| S-EPMC3188361 | biostudies-literature
Unknown Aminoacyl transfer rate dictates choice of editing pathway in threonyl-tRNA synthetase.
| S-EPMC2911285 | biostudies-literature
Unknown Predicted class-I aminoacyl tRNA synthetase-like proteins in non-ribosomal peptide synthesis.
| S-EPMC2922099 | biostudies-literature
Unknown Pyrrolysyl-tRNA synthetase, an aminoacyl-tRNA synthetase for genetic code expansion.
| S-EPMC5321558 | biostudies-literature
Unknown Metabolic origin of the fused aminoacyl-tRNA synthetase, glutamyl-prolyl-tRNA synthetase.
| S-EPMC6295713 | biostudies-literature
Unknown Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea.
| S-EPMC1560354 | biostudies-literature
Other Growth Optimized Aminoacyl-tRNA Synthetase Levels Prevent Maximal tRNA Charging
2020-07-20 | GSE141389 | GEO
Unknown Severe oxidative stress induces protein mistranslation through impairment of an aminoacyl-tRNA synthetase editing site.
| S-EPMC2840151 | biostudies-literature
Unknown Discovery of aminoacyl-tRNA synthetase activity through cell-surface display of noncanonical amino acids.
| S-EPMC1502431 | biostudies-literature