Ontology highlight
ABSTRACT:
SUBMITTER: Italia JS
PROVIDER: S-EPMC7564891 | biostudies-literature | 2020 Apr
REPOSITORIES: biostudies-literature
Italia James S JS Peeler Jennifer C JC Hillenbrand Christen M CM Latour Christopher C Weerapana Eranthie E Chatterjee Abhishek A
Nature chemical biology 20200316 4
Tyrosine sulfation is an important post-translational modification found in higher eukaryotes. Here we report an engineered tyrosyl-tRNA synthetase/tRNA pair that co-translationally incorporates O-sulfotyrosine in response to UAG codons in Escherichia coli and mammalian cells. This platform enables recombinant expression of eukaryotic proteins homogeneously sulfated at chosen sites, which was demonstrated by expressing human heparin cofactor II in mammalian cells in different states of sulfation ...[more]