Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
Membrane interactions and self-association of the TatA and TatB components of the twin-arginine translocation pathway
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DOI：
10.1016/s0014-5793(01)02904-0
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发表时间：
2001-10-05
期刊：
影响因子：
3.5
通讯作者：
Berks, BC
中科院分区：
文献类型：
--
作者：
De Leeuw, E;Porcelli, I;Berks, BC
大肠杆菌TAT系统介导带有双精氨酸信号肽的蛋白质前体的SEC非依赖性输出。Tat途径的基本成分TATA、TatB和TatC被证明是完整的膜蛋白。一旦去除了预测的N-末端跨膜螺旋，TATA就变成了一种水溶性蛋白质。相反，当类似的螺旋被删除时，同源的TatB蛋白与细胞膜的外围相互作用仍然很弱。化学交联研究表明，在天然膜环境中，TATA至少形成同源三聚体，TatB至少形成同源二聚体。大小排阻层析支持这种同-寡聚相互作用的存在。(C)2001年欧洲生化学会联合会。爱思唯尔科学公司出版。版权所有。
The Escherichia coli Tat system mediates Sec-independent export of protein precursors bearing twin-arginine signal peptides. The essential Tat pathway components TatA, TatB and TatC are shown to be integral membrane proteins. Upon removal of the predicted N-terminal transmembrane helix TatA becomes a water-soluble protein. In contrast the homologous TatB protein retains weak peripheral interactions with the cytoplasmic membrane when the analogous helix is deleted. Chemical crosslinking studies indicate that TatA forms at least homotrimers, and TatB minimally homodimers, in the native membrane environment. The presence of such homo-oligomeric interactions is supported by size exclusion chromatography. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.