CLONING AND MOLECULAR CHARACTERIZATION OF THE OMPA GENE FROM SALMONELLA-TYPHIMURIUM
CLONING AND MOLECULAR CHARACTERIZATION OF THE OMPA GENE FROM SALMONELLA-TYPHIMURIUM
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DOI：
10.1111/j.1432-1033.1983.tb07594.x
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发表时间：
1983-01-01
期刊：
影响因子：
--
通讯作者：
COLE, ST
中科院分区：
文献类型：
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作者：
FREUDL, R;COLE, ST
从鼠伤寒沙门氏菌中克隆了OmpA基因，编码外膜主要的热修饰蛋白，并对其进行了广泛的鉴定。当在大肠杆菌中表达时，该基因指导合成一种OmpA蛋白，该蛋白在功能和拓扑上与在鼠伤寒沙门氏菌中产生的蛋白没有区别，表明这两种生物的输出和膜掺入非常相似。尽管鼠伤寒沙门氏菌蛋白不能作为OmpA特异性噬菌体K3和TuII*的受体，但在F依赖的结合和对某些结肠素的吸收方面，它有效地替代了大肠杆菌多肽。对从其基因核苷酸序列预测的蛋白质的初级序列进行检查后，发现那些可能暴露在细胞表面的区域与大肠杆菌多肽的相应区域显著不同。这两种蛋白质结构上的差异被用来解释它们的生物活性的差异。
The ompA gene from S. typhimurium, encoding a major heat-modifiable protein of the outer membrane was cloned and extensively characterized. When expressed in Escherichia coli, the gene directs the synthesis of an OmpA protein which is functionally and topologically indistinguishable from that made in S. typhimurium, indicating that export and membrane incorporation are very similar in the 2 organisms. The S. typhimurium protein effectively substitutes for the E. coli polypeptide in F-dependent conjugation and in the uptake of certain colicins, although it cannot serve as the receptor for the OmpA-specific phages K3 and TuII*. On examination of the primary sequence of the protein, predicted from the nucleotide sequence of its gene, it was found that those domains likely to be exposed on the cell surface were significantly different to the corresponding regions of the E. coli polypeptide. These differences in the structure of the 2 proteins were used to interpret differences in their biological activities.