Chemical Proteomics with Sulfonyl Fluoride Probes Reveals Selective Labeling of Functional Tyrosines in Glutathione Transferases

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• 作者：Christian Gu¹ ; D. Alexander Shannon⁵ ; Tom Colby² ; Zheming Wang¹ ; Mohammed Shabab⁶ ; Selva Kumari¹ ; Joji Grace Villamor¹ ; Christopher J. McLaughlin⁵ ; Eranthie Weerapana³ ; ⁵ ; Markus Kaiser⁴ ; Benjamin F. Cravatt³ ; Renier A.L. van der Hoorn¹ ; ^{hoorn@mpipz.mpg.de}
• 刊名：Chemistry & Biology
• 出版年：2013
• 出版时间：18 April, 2013
• 年：2013
• 卷：20
• 期：4
• 页码：541-548
• 全文大小：776 K

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Summary

Chemical probes have great potential for identifying functional residues in proteins in crude proteomes. Here we studied labeling sites of chemical probes based on sulfonyl fluorides (SFs) on plant and animal proteomes. Besides serine proteases and many other proteins, SF-based probes label Tyr residues in glutathione transferases (GSTs). The labeled GSTs represent four different GST classes that share less than 30 % sequence identity. The targeted Tyr residues are located at similar positions in the promiscuous substrate binding site and are essential for GST function. The high selectivity of SF-based probes for functional Tyr residues in GSTs illustrates how these probes can be used for functional studies of GSTs and other proteins in crude proteomes.