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Article summary:
1. Tyrosine O-sulfation is a post-translational modification that regulates protein-protein interactions in extracellular space.
2. A subtractive strategy was developed to determine the sites of tyrosine O-sulfation in proteins, using acetylation and tandem mass spectrometry (MS/MS) analysis.
3. This methodology was used to identify the sites and order of sulfation of several peptides mediated by purified human tyrosylprotein sulfotransferases (TPSTs), and to determine the tyrosine sulfation sites in mouse lumican and human vitronectin.
Article analysis:
The article is generally reliable, as it provides evidence for its claims through references to other studies, such as Huttner's 1982 Nature paper on sulphation of tyrosine residues, Kehoe & Bertozzi's 2000 Chem Biol paper on tyrosine sulfation as a modulator of extracellular protein-protein interactions, Moore's 2003 J Biol Chem paper on the biology and enzymology of protein tyrosine O-sulfation, Ouyang et al.'s 1998 Proc Natl Acad Sci USA paper on purification and molecular cloning of an enzyme that catalyzes tyrosine O-sulfation, and Beisswanger et al.'s 1998 Proc Natl Acad Sci USA paper on distinct tyrosylprotein sulfotransferase genes. The article also provides clear explanations for its methods, such as the use of acetylation with S-NHSAc in the presence of imidazole at pH 7.0 to block hydroxyl groups on unsulfated tyrosines, and alkaline phosphatase treatment to distinguish between phosphorylation and sulfation of tyrosine.
However, there are some potential biases in the article that should be noted. For example, it does not explore any counterarguments or alternative theories regarding its claims about tyrosine O-sulfation being a key post-translational modification that regulates protein-protein interactions in extracellular space. Additionally, it does not provide any evidence for its claim that this methodology can be used to unambiguously determine the tyrosine sulfation sites in mouse lumican and human vitronectin; this could be addressed by providing more detailed results from experiments conducted using this methodology. Finally, while the article