Genetically encoded protein sulfation in mammalian cells

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...

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Vydané v:	Nature chemical biology Ročník 16; číslo 4; s. 379 - 382
Hlavní autori:	Italia, James S., Peeler, Jennifer C., Hillenbrand, Christen M., Latour, Christopher, Weerapana, Eranthie, Chatterjee, Abhishek
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	New York Nature Publishing Group US 01.04.2020 Nature Publishing Group
Predmet:	631/337/458 631/337/574 631/92/612 Animals Anticoagulants Biochemical Engineering Biochemistry Bioorganic Chemistry Brief Communication Cell Biology Chemistry Chemistry and Materials Science Chemistry/Food Science Codon, Terminator - metabolism Codons E coli Escherichia coli Escherichia coli - metabolism Eukaryotes Genetic Code Heparin Heparin Cofactor II - metabolism Humans Incorporation Mammalian cells Mammals Physiology Plasmids Post-translation Protein Engineering - methods Protein Processing, Post-Translational Proteins Proteins - chemistry Somatomedins - chemistry Sulfation Transfer RNA tRNA Tyrosine Tyrosine - analogs & derivatives Tyrosine - chemistry Tyrosine-tRNA ligase Tyrosine-tRNA Ligase - metabolism
ISSN:	1552-4450, 1552-4469, 1552-4469
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Popis
Shrnutí:	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. The authors used an expanded genetic code to incorporate sulfated tyrosine into specific sites of proteins expressed in E. coli and mammalian cells and showed that sulfation of tyrosine at different sites had different functions.
Bibliografia:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 14 content type line 23 Author contribution A.C. and J.S.I. designed the experiments, J.S.I. conducted all experiments, C.H. and C.L. assisted with cloning and protein expression, J.C.P. performed the MS analyses of HCII and E.W. supervised this, A.C. and J.S.I. prepared the manuscript.
ISSN:	1552-4450 1552-4469 1552-4469
DOI:	10.1038/s41589-020-0493-1