de Duve Institute, Université catholique de Louvain, Brussels, Belgium.
Proteomics. 2010 Feb;10(4):771-84. doi: 10.1002/pmic.200900461.
The cell envelope of Gram-negative bacteria is a complex macromolecular structure that is essential for their viability. Little is known on how the proteins which are secreted to the envelope fold into their unique three-dimensional structure. Several folding factors, including chaperones and protein folding catalysts involved in disulfide bond formation, have been identified in the periplasm. The characterization of these proteins has advanced our understanding of envelope biogenesis, although many fundamental questions remain unanswered. In particular, we still do not know how beta-barrel proteins are transported through the periplasm and inserted into the outer membrane. Here, we discuss the recent discoveries that have shed new light on the mechanisms that ensure the correct folding of envelope proteins. We have paid particular attention to the significant contribution of proteomic studies.
革兰氏阴性细菌的细胞包膜是一种复杂的大分子结构，对其生存能力至关重要。目前人们对于分泌到包膜中的蛋白质如何折叠成其独特的三维结构知之甚少。已经在周质中鉴定出几种折叠因子，包括参与二硫键形成的伴侣蛋白和蛋白折叠催化剂。这些蛋白质的特性描述提高了我们对包膜生物发生的理解，尽管仍有许多基本问题尚未得到解答。特别是，我们仍然不知道β桶蛋白如何穿过周质并插入外膜。在这里，我们讨论了最近的发现，这些发现为确保包膜蛋白正确折叠的机制提供了新的线索。我们特别关注蛋白质组学研究的重要贡献。
