讲座题目：Homogeneous glycoproteins for studying glycan-mediated protein folding
主讲人简介：Dr. Ning Wang日本理化学研究所细胞制御化学研究室博士后。主要研究领域：糖蛋白质量控制，体外糖蛋白折叠；已在Glycobiology, ChemBioChem等杂志发表多篇研究论文。
报告摘要：Glycosylation and folding of polypeptides in the endoplasmic reticulum (ER) are essential to lead them to biologically functional three-dimensional structures. The protein quality control system involves various carbohydrate active proteins, including enzymes, chaperones and lectins. For example, lectin chaperones calnexin (CNX) and calreticulin (CRT) specifically recognize glycopeptides exhibiting monoglucosylated glycan (GlcMan9GlcNAc2, G1M9) and assist their proper folding in cooperation with the protein disulfide isomerase. On the other hand, UDP-glucose:glycoprotein glucosyltransferase (UGGT) plays an essential role in the discrimination of folding states of the nascent glycoproteins. However, the molecular mechanism of quality control processes has not been fully investigated.
Recently, methods for chemoenzymatic synthesis of homogeneously glycosylated proteins were developed. At this moment, we report the efficient preparation of biologically active homogeneous RNases, including G1M9-RNase, M9-RNase, SCT-RNase and CT-RNase, which were used in in-vitro refolding assay. The speculated role of each glycan interacting with their recognition protein in glycoprotein folding will be discussed.
