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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >β-N-acetylglucosamine (O-GlcNAc) is part of the histone code
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β-N-acetylglucosamine (O-GlcNAc) is part of the histone code

机译：β-N-乙酰氨基葡萄糖（O-GlcNAc）是组蛋白代码的一部分

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摘要

Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions. Like phosphorylation, O-GlcNAc cycles in response to a wide variety of stimuli. Although cycling of O-GlcNAc is catalyzed by only two highly conserved enzymes, O-GlcNAc transferase (OGT), which adds the sugar, and p-N-acetylglucosaminidase (O-GlcNAcase), which hydrolyzes it, the targeting of these enzymes is highly specific and is controlled by myriad interacting subunits. Here, we demonstrate by multiple specific immunological and enzymatic approaches that histones, the proteins that package DNA within the nucleus, are O-GlcNAcylated in vivo. Histones also are substrates for OGT in vitro. We identify O-GlcNAc sites on histones H2A, H2B, and H4 using mass spectrom-etry. Finally, we show that histone O-GlcNAcylation changes during mitosis and with heat shock. Taken together, these data show that O-GlcNAc cycles dynamically on histones and can be considered part of the histone code.
机译：β-N-乙酰氨基葡萄糖（O-GlcNAc）对胞质蛋白的丝氨酸和苏氨酸残基进行动态翻译后修饰，是细胞过程（例如转录，信号传导和蛋白-蛋白相互作用）的调节剂。像磷酸化一样，O-GlcNAc会响应各种各样的刺激而循环。尽管O-GlcNAc的循环仅受两种高度保守的酶催化，添加糖的O-GlcNAc转移酶（OGT）和将其水解的pN-乙酰氨基葡糖苷酶（O-GlcNAcase）催化，但这些酶的靶向高度特异性并由无数相互作用的亚基控制。在这里，我们通过多种特定的免疫学和酶学方法证明，组蛋白是在体内将O-GlcNAcycyyl包裹的蛋白质，是包裹细胞核内DNA的蛋白质。组蛋白也是体外OGT的底物。我们使用质谱技术在组蛋白H2A，H2B和H4上确定O-GlcNAc的位点。最后，我们显示了组蛋白O-GlcNAcylation在有丝分裂和热休克期间发生变化。总而言之，这些数据表明O-GlcNAc在组蛋白上动态循环，可以被认为是组蛋白代码的一部分。

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