6wn2
Tyrosyl t-RNA Synthetase Mutant from E.coli Complexed with sulfotyrosineTyrosyl t-RNA Synthetase Mutant from E.coli Complexed with sulfotyrosine
Structural highlights
Function[A0A3Q0MY83_ECOLX] Catalyzes the attachment of tyrosine to tRNA(Tyr) in a two-step reaction: tyrosine is first activated by ATP to form Tyr-AMP and then transferred to the acceptor end of tRNA(Tyr).[HAMAP-Rule:MF_02006] Publication Abstract from PubMedProtein 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. Functional genetic encoding of sulfotyrosine in mammalian cells.,He X, Chen Y, Beltran DG, Kelly M, Ma B, Lawrie J, Wang F, Dodds E, Zhang L, Guo J, Niu W Nat Commun. 2020 Sep 24;11(1):4820. doi: 10.1038/s41467-020-18629-9. PMID:32973160[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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