L-arabinose transport systems in Escherichia coli K-12.
L-arabinose transport systems in Escherichia coli K-12.
复制标题
大肠杆菌 K-12 中的 L-阿拉伯糖转运系统。
DOI：
10.1128/jb.148.2.472-479.1981
复制
发表时间：
1981
影响因子：
3.2
通讯作者：
Schleif,R
中科院分区：
文献类型：
--
作者：
Kolodrubetz,D;Schleif,R
通过筛选在L-阿拉伯糖存在下诱导β-半乳糖苷酶的细胞，用Mu lac噬菌体分离大肠杆菌K-12的阿拉伯糖转运操纵子中的突变。然后使用标准遗传技术分离两种转运系统中任一种的许多突变。互补试验显示，只有一个基因，araE，在低亲和力的阿拉伯糖摄取系统。P1转导将araE置于lysA（60.9 min）和thyA（60.5 min）之间，并且更靠近lysA。发现高亲和力转运系统的操纵子包含两个基因：编码阿拉伯糖结合蛋白的araF和一个新基因araG。双向凝胶电泳结果表明，新鉴定的基因araG编码一种位于细胞膜上的蛋白质。在我们使用的条件下，只有araG中的缺陷可以消除高亲和力系统的摄取。
Mutations in the arabinose transport operons of Escherichia coli K-12 were isolated with the Mu lac phage by screening for cells in which beta-galactosidase is induced in the presence of L-arabinose. Standard genetic techniques were then used to isolate numerous mutations in either of the two transport systems. Complementation tests revealed only one gene, araE, in the low-affinity arabinose uptake system. P1 transduction placed araE between lysA (60.9 min) and thyA (60.5 min) and closer to lysA. The operon of the high-affinity transport system was found to contain two genes: araF, which codes for the arabinose-binding protein, and a new gene, araG. The newly identified gene, araG, was shown by two-dimensional gel electrophoresis to encode a protein which is located in the membrane. Only defects in araG could abolish uptake by the high-affinity system under the conditions we used.