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首页> 外文期刊>Biochemistry >Evolution of Antiparallel Two-Domain Membrane Proteins. Swapping Domains in the Glutamate Transporter GltS
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Evolution of Antiparallel Two-Domain Membrane Proteins. Swapping Domains in the Glutamate Transporter GltS

机译：反平行双域膜蛋白的演变。 在谷氨酸转运蛋白的交换域

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摘要

Two-domain membrane proteins are believed to have evolved through duplication and fusion events. A set of evolutionary states of the Na+-glutamate transporter of Escherichia coli was engineered. The two half-genes encoding the two domains were placed in a single operon in both orders (GltS(split)), and the split genes were fused in the reverse order compared to the original protein (GltS(swap)). The transporter halves were produced and shown to be active in Na+-coupled glutamate transport. GltS(swap) was as active as the original transporter provided that the domains were connected by a linker of the same size that connected them in the original transporter.
机译：认为双域膜蛋白通过复制和融合事件而发展。 设计了一组Na + -Glutamate Coli的Na +-谷氨酸转运蛋白的进化状态。 编码两个域的两个半基因被置于单一的操纵子中（Glts（分裂）），与原始蛋白质（GLTS（SWAP））相比，分裂基因融合。 制备转运物半部并显示在Na +耦合谷氨酸转运中活性。 GLTS（SWAP）作为原始运输器的活性，条件是域通过连接在原始运输仪中连接的相同尺寸的连接器连接。

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