Biogenesis of autotransporter proteins

将蛋白质运送到正确的细胞位置是细胞生物学的一个基本方面。自转运蛋白是革兰氏阴性细菌中的外膜蛋白家族，之所以这样命名是因为通过外膜的分泌是由这些蛋白的C-末端结构域介导的。自身转运蛋白作为粘附素、蛋白酶和介导生物膜形成的蛋白质起作用。此外，所谓的转运蛋白结构域可适于展示异源蛋白，包括疫苗表位和重金属污染解毒蛋白。在我们研究的模型自动转运蛋白中，预测C-末端区域形成β-桶，N-末端乘客结构域通过该β-桶被挤出。来自我们实验室的数据表明，蛋白质在通过转运蛋白分泌之前保持在未折叠状态。然后蛋白质在细菌表面折叠，因为它们从转运蛋白中出现。

The delivery of proteins to their correct cellular location is a fundamental aspect of cell biology. Autotransporters are a family of outer membrane proteins in Gram-negative bacteria, so named because secretion past the outer membrane is mediated by the C-terminal domain of these proteins. Autotransporters function as adhesins, proteases, and proteins that mediate biofilm formation. In addition, the so-called transporter domain can be adapted to display heterologous proteins, including vaccine epitopes and proteins to detoxify heavy-metal contamination. In the model autotransporters that we study, the C-terminal region is predicted to form a beta-barrel through which the N-terminal passenger domain is extruded. Data from our lab suggests that the proteins are maintained in an un-folded state prior to secretion via the transporter. The proteins then fold on the bacterial surface as they emerge from the transporter.