Functional genetic encoding of sulfotyrosine in mammalian cells

Xinyuan He, Yan Chen, Daisy Guiza Beltran, Maia Kelly, Bin Ma, Justin Lawrie, Feng Wang, Eric Dodds, Limei Zhang, Jiantao Guo () and Wei Niu ()
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Xinyuan He: University of Nebraska-Lincoln
Yan Chen: University of Nebraska-Lincoln
Daisy Guiza Beltran: University of Nebraska-Lincoln
Maia Kelly: University of Nebraska-Lincoln
Bin Ma: University of Nebraska-Lincoln
Justin Lawrie: University of Nebraska-Lincoln
Feng Wang: Chinese Academy of Sciences
Eric Dodds: University of Nebraska-Lincoln
Limei Zhang: University of Nebraska-Lincoln
Jiantao Guo: University of Nebraska-Lincoln
Wei Niu: University of Nebraska-Lincoln

Nature Communications, 2020, vol. 11, issue 1, 1-10

Abstract: Abstract 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.

Date: 2020
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DOI: 10.1038/s41467-020-18629-9

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