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细菌黏附中的蛋白折叠:经典单体型自转运蛋白的分泌和折叠。

Protein folding in bacterial adhesion: secretion and folding of classical monomeric autotransporters.

机构信息

Section Molecular Microbiology, Department of Molecular Cell Biology, VU University Amsterdam, De Boelelaan 1085, 1081 HV, Amsterdam, The Netherlands.

出版信息

Adv Exp Med Biol. 2011;715:125-42. doi: 10.1007/978-94-007-0940-9_8.

DOI:10.1007/978-94-007-0940-9_8
PMID:21557061
Abstract

Bacterial adhesins mediate the attachment of bacteria to their niches, such as the tissue of an infected host. Adhesins have to be transported across the cell envelope to become active and during this secretion process they fold into their final conformation. This chapter focuses on the biogenesis of the classical monomeric autotransporter proteins, which are the most ubiquitous class of secreted proteins in Gram-negative bacteria. They may function as adhesins, but other functions are also known. Autotransporter proteins have a modular structure and consist of an N-terminal signal peptide and a C-terminal translocator domain with in between the secreted passenger domain that harbours the functions. The signal peptide directs the transport across the inner membrane to the periplasm via the Sec machinery. The translocator domain inserts into the outer membrane and facilitates the transport of the passenger to the cell surface. In this chapter, I will review our current knowledge of the secretion of classical monomeric autotransporters and the methods that have been used to assess their folding during the translocation, both in vitro and in vivo.

摘要

细菌黏附素介导细菌与其生态位(如感染宿主的组织)的附着。黏附素必须穿过细胞包膜才能发挥作用,在此分泌过程中,它们折叠成最终构象。本章重点介绍经典单体型自转运蛋白的生物发生,它们是革兰氏阴性菌中最普遍的分泌蛋白类。它们可能作为黏附素发挥作用,但也有其他功能。自转运蛋白具有模块化结构,由 N 端信号肽和 C 端转运器域组成,中间是带有功能的分泌性载体域。信号肽通过 Sec 机制引导穿过内膜到周质。转运器域插入外膜并促进载体向细胞表面的运输。在本章中,我将回顾我们目前对经典单体型自转运蛋白分泌的了解,以及已用于评估其在易位过程中折叠的方法,包括体外和体内方法。

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Protein folding in bacterial adhesion: secretion and folding of classical monomeric autotransporters.细菌黏附中的蛋白折叠:经典单体型自转运蛋白的分泌和折叠。
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