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Complex glycolipid synthesis is catalyzed by different glycosyltransferases resident of the Golgi complex. Most of them are type II membrane proteins comprising a lumenal, C-terminal domain linked to an N-terminal domain (Ntd) constituted by a short cytoplasmic tail (ct), a transmembrane, and a lumenal stem regions. They concentrate selectively in different sub-Golgi compartments, in an overlapped manner, acting in succession in the addition of sugars to acceptor glycolipids. The Ntds are sufficient to localize glycosyltransferases in the Golgi complex, but it is not clear whether they also confer selective concentration in sub-Golgi compartments. Here, we studied whether the Ntd of SialT2, localized in the proximal Golgi, and the one of GalNAcT, a trans/TGN Golgi-concentrated enzyme, concentrate reporter proteins in the corresponding sub-Golgi compartment. The sub-Golgi concentration of the Ntds fused to spectral variants of the GFP was determined in CHO-K1 cells from their behavior upon addition of brefeldin A. Fluorescence microscopy and subcellular fractionation showed that the SialT2 Ntd concentrates in a proximal sub-Golgi compartment - and that of GalNAcT in TGN elements. Exchanging the transmembrane region and the cts of SialT2 and GalNAcT indicates that information for proximal or distal Golgi concentration is associated with the cts.  相似文献   
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研究表明,许多神经退行性疾病都与蛋白质在高尔基体中的定位有关,因此,正确识别亚高尔基体蛋白质对相关疾病药物的研制有一定帮助,本文建立了两类亚高尔基体蛋白质数据集,提取了氨基酸组分信息、联合三联体信息、平均化学位移、基因本体注释信息等特征信息,利用支持向量机算法进行预测,基于5-折交叉检验下总体预测成功率为87.43%。  相似文献   
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