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菌外膜蛋白的一个家族，之所以如此命名，是因为通过外膜的分泌是由这些蛋白的c端结构域介导的。自转运蛋白的功能包括粘附素、蛋白酶和介导生物膜形成的蛋白质。此外，所谓的转运体结构域可以适应显示异源蛋白，包括疫苗表位和解毒重金属污染的蛋白质。在我们研究的模型自动转运蛋白中，预测c端区域形成β -桶，通过该桶，n端乘客域被挤出。我们实验室的数据表明，在通过转运体分泌之前，蛋白质保持在未折叠状态。当蛋白质从转运体中出来时，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.