Mercurio A, Manning P A
Mol Gen Genet. 1985;200(3):472-5. doi: 10.1007/BF00425733.
The cellular location of the haemolysin of Vibrio cholerae El Tor strain 017 has been analyzed. This protein is found both in the periplasmic space and the extracellular medium in Vibrio cholerae. However, when the cloned gene, present on plasmid pPM431, is introduced into E. coli K-12 this protein remains localized predominantly in the periplasmic space with no activity detected in the extracellular medium. Mutants of E. coli K-12 (tolA and tolB) which leak periplasmic proteins mimic excretion and release the haemolysin into the growth medium. Secretion of haemolysin into the periplasm is independent of perA (envZ) and in fact, mutants in perA (envZ) harbouring pPM431 show hyperproduction of periplasmic haemolysin. These results in conjunction with those for other V. cholerae extracellular proteins suggest that although E. coli K-12 can secrete these proteins into the periplasm, it lacks a specific excretion mechanism, present in V. cholerae, for the release of soluble proteins into the growth medium.
已对霍乱弧菌埃尔托生物型017菌株溶血素的细胞定位进行了分析。在霍乱弧菌中,这种蛋白质存在于周质空间和细胞外培养基中。然而,当存在于质粒pPM431上的克隆基因被导入大肠杆菌K-12时,这种蛋白质主要仍定位于周质空间,在细胞外培养基中未检测到活性。大肠杆菌K-12的突变体(tolA和tolB)会泄漏周质蛋白,模拟排泄并将溶血素释放到生长培养基中。溶血素分泌到周质中与perA(envZ)无关,事实上,携带pPM431的perA(envZ)突变体显示周质溶血素超量产生。这些结果与其他霍乱弧菌细胞外蛋白的结果一起表明,虽然大肠杆菌K-12可以将这些蛋白质分泌到周质中,但它缺乏霍乱弧菌中存在的将可溶性蛋白质释放到生长培养基中的特定排泄机制。