The identification and molecular function of nuclear glycosyl transferase complex

在本研究中，我们重点研究了O-linked N-acetylglucosamine transferase（OGT）的分子功能，该酶在我们之前的研究中被鉴定为核受体（NR）介导转录的共激活因子。为了了解OGT激活染色质转录的分子基础，我们通过亲和纯化纯化了它的相互作用伙伴，并鉴定了包括组蛋白甲基转移酶在内的几个染色质调节因子。此外，我们发现组蛋白是一种新的OGT底物。总之，这一修饰可能是调控真核生物基因表达网络的重要表观遗传密码。

In this research, we focused on the molecular function of O-linked N-acetylglucosamine transferase(OGT), which was identified as a co-activator of nuclear receptor(NR)-mediated transcription in our previous study. To understand the molecular basis for OGT to activate transcription from chromatin, we purified its interacting partners by affinity purification, and identified several chromatin regulatory factors including histone methyltransferases. In addition, we found that histone was a novel substrate for OGT. Together, this modification might be a substantial epigenetic code for the regulation of eukaryotic gene expression network.