Journal
NATURE COMMUNICATIONS
Volume 11, Issue 1, Pages -Publisher
NATURE RESEARCH
DOI: 10.1038/s41467-020-18629-9
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Funding
- U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences [DE-AC02-76SF00515]
- University of Nebraska-Lincoln
- National Science Foundation [CBET 1805528, MCB 1553041, CLP 1846908]
- National Institute of Health [1R01AI111862]
- National Institute of Health (Nebraska Redox Biology Center) [P30 GM103335]
- MacNair Scholarship from University of Nebraska-Lincoln
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Protein tyrosine O-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions 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. Protein tyrosine O-sulfation is crucial for biomolecular interactions. Here the authors report in vitro engineering and in vivo validation of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells.
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