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Substrate-transporter complexes in the twin-arginine protein transport system

双精氨酸蛋白转运系统中的底物-转运蛋白复合物

基本信息

批准号：
BB/F02150X/1
负责人：
Benjamin Berks
金额：
$ 47.63万
依托单位：
University of Oxford
依托单位国家：
英国
项目类别：
Research Grant
财政年份：
2009
资助国家：
英国
起止时间：
2009 至无数据
项目状态：
已结题

来源：
https://gtr.ukri.org/projects?ref=BB%2FF02150X%2F1
关键词：
Substrate transporter complexes twin arginine

项目摘要

Some proteins operate on the outside of the bacterial cell, for example the toxins produced by bacterial pathogens. Since all proteins are made inside the bacterium the extracellular proteins must be moved out of the cell across the normally impermeable cell membrane. This task is carried out by machines termed protein transporters that are located in the cell membrane. One type of transporter moves unfolded proteins, threading them across the membrane like string through the eye of a needle. By contrast, a second type of transporter, which we term the Tat system, moves folded proteins across the membrane. This is much more challenging than threading and so it is thought that the Tat system operates by an unusual mechanism. The Tat system is required for many bacterial processes including energy generation, cell division, pathogenesis, and the nitrogen-fixing symbiosis of soil bacteria with plants. The Tat protein transport system is not only found in bacteria but is also present in the chloroplasts of plants where it is essential to form and maintain the proteins required to carry out photosynthesis. The heart of the Tat system is a complex formed by two proteins called TatB and TatC. This complex sits in the cell membrane and recognises and binds the proteins that are to be transported. It then binds another protein called TatA to form the active transporter. This project aims to characterise the complexes formed between the Tat components and the transported protein in more detail with the aim of increasing our understanding of the unusual mechanism of the Tat system. The Tat system is a possible drug target because it is required for bacterial pathogenesis but is not found in humans. It is also of biotechnological interest because it could be utilised to secrete useful protein products.

一些蛋白质在细菌细胞的外部起作用，例如细菌病原体产生的毒素。由于所有的蛋白质都是在细菌内部制造的，因此胞外蛋白质必须穿过通常不可渗透的细胞膜移出细胞。这一任务是由位于细胞膜上的蛋白质转运蛋白完成的。一种类型的转运蛋白移动未折叠的蛋白质，将它们穿过细胞膜，就像穿过针眼的线一样。相比之下，第二种类型的转运蛋白，我们称之为达特系统，将折叠的蛋白质跨膜移动。这比线程化更具挑战性，因此人们认为达特系统通过一种不寻常的机制运行。达特系统是许多细菌过程所必需的，包括能量产生、细胞分裂、致病以及土壤细菌与植物的固氮共生。达特蛋白转运系统不仅存在于细菌中，而且也存在于植物的叶绿体中，在叶绿体中形成和维持进行光合作用所需的蛋白质是必需的。达特系统的核心是由两种名为TatB和TatC的蛋白质形成的复合物。这种复合物位于细胞膜中，识别并结合要运输的蛋白质。然后，它结合另一种称为TatA的蛋白质，形成活性转运蛋白。本项目旨在更详细地阐明达特组分与转运蛋白之间形成的复合物，目的是增加我们对达特系统的不寻常机制的理解。达特系统是一个可能的药物靶点，因为它是细菌致病所必需的，但在人类中没有发现。它也是生物技术的兴趣，因为它可以用来分泌有用的蛋白质产品。

项目成果

期刊论文数量（5）

专著数量（0）

科研奖励数量（0）

会议论文数量（0）

专利数量（0）

A complex iron-calcium cofactor catalyzing phosphotransfer chemistry.

DOI：
10.1126/science.1254237
发表时间：
2014-09-05
期刊：
Science (New York, N.Y.)
影响因子：
0
作者：
Yong SC;Roversi P;Lillington J;Rodriguez F;Krehenbrink M;Zeldin OB;Garman EF;Lea SM;Berks BC
通讯作者：
Berks BC

Structure of the TatC core of the twin-arginine protein transport system.

DOI：
10.1038/nature11683
发表时间：
2012-12-13
期刊：
Nature
影响因子：
64.8
作者：
通讯作者：

Molecular dissection of TatC defines critical regions essential for protein transport and a TatB-TatC contact site.

DOI：
10.1111/j.1365-2958.2012.08151.x
发表时间：
2012-09
期刊：
Molecular microbiology
影响因子：
3.6
作者：
Kneuper H;Maldonado B;Jäger F;Krehenbrink M;Buchanan G;Keller R;Müller M;Berks BC;Palmer T
通讯作者：
Palmer T