Hikita C, Satake Y, Yamada H, Mizuno T, Mizushima S
Res Microbiol. 1989 Mar-Apr;140(3):177-90. doi: 10.1016/0923-2508(89)90074-0.
The roles of submolecular regions of OmpF and OmpC, major outer membrane proteins of Escherichia coli, as concerns their biogenesis, structure and function were studied using a large number of chimeric genes constructed from the ompF and ompC genes through single or double homologous in vivo recombination. When recombination between the two genes took place at certain regions of their central regions, no chimeric protein was detected, irrespective of whether the amino-terminal and carboxy-terminal regions were derived from OmpF or OmpC. Biochemical studies revealed that these proteins were synthesized and exported across the cytoplasmic membrane normally, but that they were not properly assembled into the outer membrane and hence were degraded rapidly. Characterization of these chimeric proteins, in which recombination between OmpF and OmpC took place once or twice, suggested that the central region of each of these proteins plays an important role in the respective assembly, whereas the roles of the amino-terminal and carboxy-terminal regions may be marginal. Functional characterization of these chimeric proteins revealed the regions important for the receptor functions of OmpF and OmpC for phages TuIa and TuIb, respectively.
利用通过单重或双重体内同源重组从ompF和ompC基因构建的大量嵌合基因，研究了大肠杆菌主要外膜蛋白OmpF和OmpC的亚分子区域在其生物发生、结构和功能方面的作用。当两个基因在其中心区域的某些区域发生重组时，无论氨基末端和羧基末端区域是源自OmpF还是OmpC，均未检测到嵌合蛋白。生化研究表明，这些蛋白能够正常合成并跨细胞质膜输出，但它们没有正确组装到外膜中，因此被迅速降解。对这些OmpF和OmpC之间发生一次或两次重组的嵌合蛋白的表征表明，这些蛋白各自的中心区域在各自的组装中起重要作用，而氨基末端和羧基末端区域的作用可能较小。对这些嵌合蛋白的功能表征揭示了分别对OmpF和OmpC作为噬菌体TuIa和TuIb受体功能而言重要的区域。
