Molecular Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Groningen, The Netherlands.
Biochemistry. 2010 Jul 27;49(29):5972-4. doi: 10.1021/bi100918j.
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.
双域膜蛋白被认为是通过复制和融合事件进化而来的。设计了一组大肠杆菌 Na(+)-谷氨酸转运蛋白的进化状态。这两个编码两个结构域的半基因被放在单个操纵子中，并且这两个半基因的融合顺序与原始蛋白相反（GltS(swap)）。转运体的两半被产生并被证明在 Na(+)-偶联谷氨酸转运中是活跃的。只要连接两个结构域的连接子与原始转运体中的连接子大小相同，那么 GltS(swap)就像原始转运体一样活跃。
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