Ontology highlight
ABSTRACT:
SUBMITTER: Zeng Y
PROVIDER: S-EPMC4167342 | biostudies-literature | 2014 Aug
REPOSITORIES: biostudies-literature
Chembiochem : a European journal of chemical biology 20140708 12
The rare AGG codon in Escherichia coli has been reassigned to code non-canonical amino acids (ncAAs) by using the PylRS-tRNA(Pyl)(CCU) pair. When N(ε) -alloc-lysine was used as a PylRS substrate, almost quantitative occupancy of N(ε) -alloc-lysine at an AGG codon site was achieved in minimal medium. ncAAs can be potentially incorporated at the AGG codon with varying efficiencies, depending on their activities towards corresponding enzymes. As AGG is a sense codon, the approach reported here reso ...[more]