Chemical and Biomolecular Engineering, Department of
ORCID IDs
http://orcid.org/0000-0002-9383-1107
http://orcid.org/0000-0003-2980-4646
http://orcid.org/0000-0001-6807-5103
http://orcid.org/0000-0001-6983-9953
http://orcid.org/0000-0003-3826-1276
Date of this Version
2020
Document Type
Article
Citation
ATURE COMMUNICATIONS | (2020)11:4820 | https://doi.org/10.1038/s41467-020-18629-9 | www.nature.com/naturecommunications
Abstract
Protein tyrosine O-sulfation (PTS) plays a crucial role in extracellular biomolecular interac- tions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.
Comments
The Author(s) 2020