Hediger M A, Turk E, Wright E M
Department of Physiology, University of California, Los Angeles School of Medicine 90024-1751.
Proc Natl Acad Sci U S A. 1989 Aug;86(15):5748-52. doi: 10.1073/pnas.86.15.5748.
Cotransport proteins are responsible for the active accumulation of organic substrates in cells. Na+ gradients provide the driving force for uptake of most substrates into eukaryotes and for a few substrates in some prokaryotes. We report here the cloning and sequencing of the human intestinal Na+/glucose cotransporter (SGLT1) and compare its structure with other cloned transporters. At the DNA level and the predicted amino acid and secondary structure levels, close homology is evident between the human and rabbit intestinal Na+/glucose cotransporters, and a significant homology is found between these and the Escherichia coli Na+/proline cotransporter (putP). No homology is detectible with other known proteins. We infer from these results that the mammalian Na+/glucose and prokaryote Na+/proline cotransporters share a common ancestral gene.
协同转运蛋白负责细胞中有机底物的主动积累。钠离子梯度为大多数底物进入真核生物以及某些原核生物中的少数底物提供了摄取的驱动力。我们在此报告人类肠道钠/葡萄糖协同转运蛋白(SGLT1)的克隆和测序,并将其结构与其他克隆的转运蛋白进行比较。在DNA水平、预测的氨基酸和二级结构水平上,人类和兔肠道钠/葡萄糖协同转运蛋白之间存在明显的同源性,并且在这些与大肠杆菌钠/脯氨酸协同转运蛋白(putP)之间发现了显著的同源性。与其他已知蛋白质未检测到同源性。我们从这些结果推断,哺乳动物的钠/葡萄糖和原核生物的钠/脯氨酸协同转运蛋白共享一个共同的祖先基因。