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New insights into the substrate specificities of proton-coupled oligopeptide transporters from E. coli by a pH sensitive assay

机译:通过pH敏感测定对大肠杆菌中质子偶联的寡肽转运蛋白的底物特异性的新见解

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Proton-coupled oligopeptide transporters (POTs) are secondary active transporters that facilitate di- and tripeptide uptake by coupling it to an inward directed proton electrochemical gradient. Here the substrate specificities of Escherichia coli POTs YdgR, YhiP and YjdL were investigated by means of a label free transport assay using the hydrophilic pH sensitive dye pyranine and POT overexpressing E. coli cells. The results confirm and extend the functional knowledge on E. coli POTs. In contrast to previous assumptions, alanine and trialanine appears to be substrates of YjdL, albeit poor compared to dipeptides. Similarly tetraalanine apparently is a substrate of both YdgR and YhiP.
机译:质子偶联的寡肽转运蛋白(POT)是次级活性转运蛋白,可通过将其与内向质子电化学梯度偶联来促进二肽和三肽的摄取。在此,通过使用亲水性pH敏感染料吡喃和过表达POT的大肠杆菌细胞的无标记转运测定法研究了大肠杆菌POTs YdgR,YhiP和YjdL的底物特异性。结果证实并扩展了对大肠杆菌POT的功能知识。与以前的假设相反,丙氨酸和三氢嘌呤似乎是YjdL的底物,尽管与二肽相比差。类似地,四丙氨酸显然是YdgR和YhiP的底物。

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