Gething M J, McCammon K, Sambrook J
Cell. 1986 Sep 12;46(6):939-50. doi: 10.1016/0092-8674(86)90076-0.
The hemagglutinin of influenza virus is synthesized as a monomeric subunit that is cotranslationally translocated across the membrane of the rough endoplasmic reticulum. We show that folding and assembly of hemagglutinin monomers into trimeric structures takes approximately 7-10 min and is completed before the protein leaves the endoplasmic reticulum. Mutants of hemagglutinin that fail to be transported from the endoplasmic reticulum are blocked at different stages of the folding pathway. Unfolded molecules of hemagglutinin are associated with a cellular protein of 77 kd that has been shown previously to bind to IgG heavy chain in the endoplasmic reticulum of certain myelomas. We discuss why assembly of native structures is required for transport of proteins through the exocytotic pathway.
流感病毒的血凝素作为单体亚基合成，在翻译过程中跨糙面内质网膜易位。我们发现，血凝素单体折叠并组装成三聚体结构大约需要7 - 10分钟，且在蛋白质离开内质网之前完成。无法从内质网转运的血凝素突变体在折叠途径的不同阶段受阻。未折叠的血凝素分子与一种77kd的细胞蛋白相关，该蛋白先前已被证明在某些骨髓瘤的内质网中与IgG重链结合。我们讨论了为什么天然结构的组装是蛋白质通过胞吐途径转运所必需的。
