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。自体转运蛋白是革兰氏阴性细菌的外膜蛋白家族，之所以被称为自体转运蛋白，是因为外膜外的分泌是由这些蛋白的C末端结构域介导的。自体转运蛋白的功能是粘附素、蛋白酶和蛋白质，它们介导生物膜的形成。此外，所谓的转运体结构域可以被改造成展示异源蛋白质，包括疫苗表位和解毒重金属污染的蛋白质。在我们研究的模型中，C-末端区域被预测形成一个贝塔桶，N-末端乘客结构域通过它被挤出。来自我们实验室的数据表明，在通过转运蛋白分泌之前，蛋白质保持在未折叠状态。然后，当这些蛋白质从转运体中出现时，它们会在细菌表面折叠。

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.