COTRANSLATIONAL FOLDING AND CALNEXIN BINDING DURING GLYCOPROTEIN-SYNTHESIS
COTRANSLATIONAL FOLDING AND CALNEXIN BINDING DURING GLYCOPROTEIN-SYNTHESIS
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DOI：
10.1073/pnas.92.14.6229
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发表时间：
1995-07-03
影响因子：
11.1
通讯作者：
HELENIUS, A
中科院分区：
文献类型：
--
作者：
CHEN, W;HELENIUS, J;HELENIUS, A
为了分析活细胞内质网中流感血凝素的共翻译折叠，我们使用短脉冲放射性标记，然后进行免疫沉淀，并使用二维 SDS/聚丙烯酰胺凝胶系统进行分析，该系统在第一维为非还原性，在第二维为还原性，分离了不同长度和氧化态的新生糖多肽。获得了共翻译二硫键形成、构象表位生成、N-连接糖基化和钙连接蛋白的寡糖依赖性结合的证据，钙连接蛋白是一种膜结合分子伴侣，通过部分葡萄糖修饰的寡糖与不完全折叠的糖蛋白结合。当糖基化或寡糖修饰受到抑制时，折叠途径受到干扰，这表明 N-连接寡糖和钙连接蛋白在翻译过程中的作用。血凝素。
To analyze cotranslational folding of influenza hemagglutinin in the endoplasmic reticulum of live cells, we used short pulses of radiolabeling followed by immunoprecipitation and analysis with a two-dimensional SDS/polyacrylamide gel system which was nonreducing in the first dimension and reducing in the second, It separated nascent glycopolypeptides of different length and oxidation state. Evidence was obtained for cotranslational disulfide formation, generation of conformational epitopes, N-linked glycosylation, and oligosaccharide-dependent binding of calnexin, a membrane-bound chaperone that binds to incompletely folded glycoproteins via partially glucose-trimmed oligosaccharides, When glycosylation or oligosaccharide trimming was inhibited, the folding pathway was perturbed, suggesting a role for N-linked oligosaccharides and calnexin during translation of hemagglutinin.