Wang Siyao, Corcilius Leo, Sharp Phillip P, Rajkovic Andrei, Ibba Michael, Parker Benjamin L, Payne Richard J
School of Chemistry , The University of Sydney , Sydney , NSW 2006 , Australia . Email:
ACRF Chemical Biology Division , Walter and Eliza Hall Institute of Medical Research , 1G Royal Parade , VIC3052 , Australia.
Chem Sci. 2017 Mar 1;8(3):2296-2302. doi: 10.1039/c6sc03847f. Epub 2016 Dec 12.
A new class of N-linked protein glycosylation - arginine rhamnosylation - has recently been discovered as a critical modification for the function of bacterial elongation factor P (EF-P). Herein, we describe the synthesis of suitably protected α- and β-rhamnosylated arginine amino acid "cassettes" that can be directly installed into rhamnosylated peptides. Preparation of a proteolytic fragment of EF-P bearing both α- and β-rhamnosylated arginine enabled the unequivocal determination of the native glycosidic linkage to be α through 2D NMR and nano-UHPLC-tandem mass spectrometry studies.
最近发现了一类新的N-连接蛋白糖基化——精氨酸鼠李糖基化——是细菌延伸因子P（EF-P）功能的关键修饰。在此，我们描述了可直接安装到鼠李糖基化肽中的适当保护的α-和β-鼠李糖基化精氨酸氨基酸“盒”的合成。制备同时含有α-和β-鼠李糖基化精氨酸的EF-P蛋白水解片段，通过二维核磁共振和纳升超高效液相色谱-串联质谱研究，明确确定了天然糖苷键为α型。
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