Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling
Artificial Cysteine S-Glycosylation Induced by Per-O-Acetylated Unnatural Monosaccharides during Metabolic Glycan Labeling
复制标题
代谢聚糖标记过程中全 O 乙酰化非天然单糖诱导的人工半胱氨酸 S-糖基化。
DOI：
10.1002/anie.201711710
复制
发表时间：
2018-02-12
影响因子：
16.6
通讯作者：
Chen, Xing
中科院分区：
文献类型：
--
作者：
Qin, Wei;Qin, Ke;Chen, Xing
描述了全 O-乙酰化单糖对各种蛋白质中的半胱氨酸残基进行意想不到的非酶促 S-糖基化。这种人工 S-糖基化极大地损害了活细胞中全 O-乙酰化叠氮基和炔基糖标记代谢聚糖的特异性和有效性，几十年来，这一点在该领域一直被忽视。事实证明，使用非乙酰化非天然糖可以避免伪影的形成，并且已使用 N-叠氮乙酰半乳糖胺 (GalNAz) 组装了 HeLa 细胞中 O-GlcNAc 蛋白和 O-GlcNAc 位点的正确列表。
The unexpected, non-enzymatic S-glycosylation of cysteine residues in various proteins by per-O-acetylated monosaccharides is described. This artificial S-glycosylation greatly compromises the specificity and validity of metabolic glycan labeling in living cells by per-O-acetylated azido and alkynyl sugars, which has been overlooked in the field for decades. It is demonstrated that the use of unacetylated unnatural sugars can avoid the artifact formation and a corrected list of O-GlcNAcylated proteins and O-GlcNAc sites in HeLa cells has been assembled by using N-azidoacetylgalactosamine (GalNAz).