Ontology highlight
ABSTRACT:
SUBMITTER: Link AJ
PROVIDER: S-EPMC1502431 | biostudies-literature | 2006 Jul
REPOSITORIES: biostudies-literature
Link A James AJ Vink Mandy K S MKS Agard Nicholas J NJ Prescher Jennifer A JA Bertozzi Carolyn R CR Tirrell David A DA
Proceedings of the National Academy of Sciences of the United States of America 20060626 27
The incorporation of noncanonical amino acids into recombinant proteins in Escherichia coli can be facilitated by the introduction of new aminoacyl-tRNA synthetase activity into the expression host. We describe here a screening procedure for the identification of new aminoacyl-tRNA synthetase activity based on the cell surface display of noncanonical amino acids. Screening of a saturation mutagenesis library of the E. coli methionyl-tRNA synthetase (MetRS) led to the discovery of three MetRS mut ...[more]