van Dijl Jan Maarten, Braun Peter G, Robinson Colin, Quax Wim J, Antelmann Haike, Hecker Michael, Müller Jörg, Tjalsma Harold, Bron Sierd, Jongbloed Jan D H
Department of Pharmaceutical Biology, University of Groningen, A. Deusinglaan 1, The Netherlands.
J Biotechnol. 2002 Sep 25;98(2-3):243-54. doi: 10.1016/s0168-1656(02)00135-9.
Protein secretion from Bacillus species is a major industrial production tool with a market of over $1 billion per year. However, standard export technologies, based on the well-characterised general secretory (Sec) pathway, are frequently inapplicable for the production of proteins. The recently discovered twin-arginine translocation (Tat) pathway offers additional potential to transport proteins. Here we review the use of functional genomic and proteomic approaches to explore the Tat pathway of Bacillus subtilis. The properties of Tat pathway components and the twin-arginine signal peptides that direct proteins into this pathway are discussed. Where appropriate, a comparison is made with Tat systems from other organism, such as Escherichia coli. Recent findings with the latter organism in particular provide proof-of-principle that the Tat pathway can be exploited for the production of Sec-incompatible proteins.
芽孢杆菌属的蛋白质分泌是一种主要的工业生产手段，每年的市场规模超过10亿美元。然而，基于已充分表征的一般分泌（Sec）途径的标准输出技术，通常不适用于蛋白质的生产。最近发现的双精氨酸转运（Tat）途径为蛋白质运输提供了额外的潜力。在此，我们综述了利用功能基因组学和蛋白质组学方法探索枯草芽孢杆菌Tat途径的情况。讨论了Tat途径组分的特性以及将蛋白质导入该途径的双精氨酸信号肽。在适当的地方，与其他生物体（如大肠杆菌）的Tat系统进行了比较。特别是后者生物体的最新发现提供了原理证明，即Tat途径可用于生产与Sec不兼容的蛋白质。
