Evans Margery L, Chapman Matthew R
Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA.
Department of Molecular, Cellular and Developmental Biology, University of Michigan, 830 North University, Ann Arbor, MI 48109, USA.
Biochim Biophys Acta. 2014 Aug;1843(8):1551-8. doi: 10.1016/j.bbamcr.2013.09.010. Epub 2013 Sep 27.
Many bacteria assemble extracellular amyloid fibers on their cell surface. Secretion of proteins across membranes and the assembly of complex macromolecular structures must be highly coordinated to avoid the accumulation of potentially toxic intracellular protein aggregates. Extracellular amyloid fiber assembly poses an even greater threat to cellular health due to the highly aggregative nature of amyloids and the inherent toxicity of amyloid assembly intermediates. Therefore, temporal and spatial control of amyloid protein secretion is paramount. The biogenesis and assembly of the extracellular bacterial amyloid curli is an ideal system for studying how bacteria cope with the many challenges of controlled and ordered amyloid assembly. Here, we review the recent progress in the curli field that has made curli biogenesis one of the best-understood functional amyloid assembly pathways. This article is part of a Special Issue entitled: Protein trafficking and secretion in bacteria. Guest Editors: Anastassios Economou and Ross Dalbey.
许多细菌在其细胞表面组装细胞外淀粉样纤维。蛋白质跨膜分泌以及复杂大分子结构的组装必须高度协调，以避免潜在有毒的细胞内蛋白质聚集体的积累。由于淀粉样蛋白的高度聚集性质以及淀粉样蛋白组装中间体的内在毒性，细胞外淀粉样纤维组装对细胞健康构成了更大的威胁。因此，淀粉样蛋白分泌的时间和空间控制至关重要。细胞外细菌淀粉样蛋白卷曲纤维的生物发生和组装是研究细菌如何应对受控和有序淀粉样蛋白组装诸多挑战的理想系统。在此，我们综述了卷曲纤维领域的最新进展，这些进展使卷曲纤维生物发生成为最被理解的功能性淀粉样蛋白组装途径之一。本文是名为：细菌中的蛋白质运输和分泌的特刊的一部分。客座编辑：阿纳斯塔西奥斯·埃科诺莫和罗斯·达尔贝。
