MalF和MalG蛋白对底物和周质结合蛋白识别的遗传证据，这两种蛋白是大肠杆菌麦芽糖转运系统的细胞质膜成分。
Genetic evidence for substrate and periplasmic-binding-protein recognition by the MalF and MalG proteins, cytoplasmic membrane components of the Escherichia coli maltose transport system.
作者信息
Treptow N A, Shuman H A
出版信息
J Bacteriol. 1985 Aug;163(2):654-60. doi: 10.1128/jb.163.2.654-660.1985.
Abstract
We isolated mutants of Escherichia coli in which the maltose-binding protein (MBP) is no longer required for growth on maltose as the sole source of carbon and energy. These mutants were selected as Mal+ revertants of a strain which carries a deletion of the MBP structural gene, malE. In one class of these mutants, maltose is transported into the cell independently of MBP by the remaining components of the maltose system. The mutations in these strains map in either malF or malG. These genes code for two of the cytoplasmic membrane components of the maltose transport system. In some of the mutants, MBP actually inhibits maltose transport. We demonstrate that these mutants still transport maltose actively and in a stereospecific manner. These results suggest that the malF and malG mutations result in exposure of a substrate recognition site that is usually available only to substrates bound to MBP.
摘要
我们分离出了大肠杆菌的突变体，在这些突变体中，麦芽糖结合蛋白（MBP）对于以麦芽糖作为唯一碳源和能源的生长不再是必需的。这些突变体是从携带MBP结构基因malE缺失的菌株中筛选出的Mal+回复突变体。在这类突变体的一个类别中，麦芽糖通过麦芽糖系统的其余组分独立于MBP转运到细胞中。这些菌株中的突变定位于malF或malG。这些基因编码麦芽糖转运系统的两个细胞质膜组分。在一些突变体中，MBP实际上抑制麦芽糖转运。我们证明这些突变体仍然以立体特异性方式主动转运麦芽糖。这些结果表明，malF和malG突变导致了一个底物识别位点的暴露，该位点通常仅对与MBP结合的底物可用。
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