使用磺酰氟探针的化学蛋白质组学揭示了谷胱甘肽转移酶中功能性酪氨酸的选择性标记。
Chemical proteomics with sulfonyl fluoride probes reveals selective labeling of functional tyrosines in glutathione transferases.
作者信息
Gu Christian, Shannon D Alexander, Colby Tom, Wang Zheming, Shabab Mohammed, Kumari Selva, Villamor Joji Grace, McLaughlin Christopher J, Weerapana Eranthie, Kaiser Markus, Cravatt Benjamin F, van der Hoorn Renier A L
机构信息
The Plant Chemetics Laboratory, Max Planck Institute for Plant Breeding Research, Carl-von-Linne Weg 10, 50829 Cologne, Germany.
出版信息
Chem Biol. 2013 Apr 18;20(4):541-8. doi: 10.1016/j.chembiol.2013.01.016.
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.
化学探针在识别粗蛋白质组中蛋白质的功能残基方面具有巨大潜力。在此，我们研究了基于磺酰氟（SFs）的化学探针在植物和动物蛋白质组上的标记位点。除了丝氨酸蛋白酶和许多其他蛋白质外，基于SF的探针还能标记谷胱甘肽转移酶（GSTs）中的酪氨酸（Tyr）残基。被标记的GSTs代表了四种不同的GST类别，它们的序列同一性低于30%。靶向的Tyr残基位于混杂底物结合位点的相似位置，并且对于GST功能至关重要。基于SF的探针对GSTs中功能性Tyr残基的高选择性说明了这些探针可如何用于粗蛋白质组中GSTs和其他蛋白质的功能研究。
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