Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
Oligomeric properties and signal peptide binding by Escherichia coli Tat protein transport complexes
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DOI：
10.1016/s0022-2836(02)00820-3
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发表时间：
2002-10-04
影响因子：
5.6
通讯作者：
Berks, BC
中科院分区：
文献类型：
--
作者：
de Leeuw, E;Granjon, T;Berks, BC
大肠杆菌TAT装置是一种蛋白质转运系统，用于将折叠的蛋白质通过内膜输出。完整的膜蛋白TATA、TatB和TatC是该途径的重要组成部分。底物蛋白通过带有共同的双精氨酸序列基序的特殊N-末端信号肽被定向到TAT装置。在这里，我们系统地研究了可以从高产菌株中纯化的TAT复合体。我们的数据表明，TATA、TatB和TatC蛋白至少存在于洗涤剂溶液中的两种主要类型的高分子复合体中，一种主要由TATA组成，但含有少量的TatB，另一种以TatBC为单位，但也含有一些TATA蛋白。后者被证明能够与TAT信号肽结合。使用另一种纯化策略，我们证明了分离出含有高摩尔过剩的TATA组分的TatABC络合物是可能的。(C)2002爱思唯尔科学有限公司。保留所有权利。
The Escherichia coli Tat apparatus is a protein translocation system that serves to export folded proteins across the inner membrane. The integral membrane proteins TatA, TatB and TatC are essential components of this pathway. Substrate proteins are directed to the Tat apparatus by specialized N-terminal signal peptides bearing a consensus twin-arginine sequence motif. Here we have systematically examined the Tat complexes that can be purified from overproducing strains. Our data suggest that the TatA, TatB and TatC proteins are found in at least two major types of high molecular mass complex in detergent solution, one consisting predominantly of TatA but with a small quantity of TatB, and the other based on a TatBC unit but also containing some TatA protein. The latter complex is shown to be capable of binding a Tat signal peptide. Using an alternative purification strategy we show that it is possible to isolate a TatABC complex containing a high molar excess of the TatA component. (C) 2002 Elsevier Science Ltd. All rights reserved.