Seiffer D, Klein J R, Plapp R
Fachbereich Biologie, Abteilung Mikrobiologie, Universität Kaiserslautern, FRG.
FEMS Microbiol Lett. 1993 Mar 1;107(2-3):175-8. doi: 10.1111/j.1574-6968.1993.tb06026.x.
A gene product with an apparent molecular mass of approximately 39,000 Da can be identified in the cytoplasmic membrane of Escherichia coli upon expression of cloned envC. In this communication we report that the product was labelled with [3H]glycerol and [3H]palmitic acid, and a precursor molecule of increased molecular mass was accumulated when cells were treated with globomycin, a specific inhibitor for the prolipoprotein signal peptidase. The same precursor molecule was encoded by an envC mutant gene, in which the cysteine residue in a pentapeptide sequence, Leu-Ile-Ala-Gly-Cys24 within the amino terminal region of EnvC, was replaced by tryptophane (Trp24). This protein was not labelled with [3H]glycerol. The results demonstrate that the envC gene product represents a new lipoprotein of the cytoplasmic membrane of E. coli.
当克隆的envC基因表达时,在大肠杆菌的细胞质膜中可鉴定出一种表观分子量约为39,000 Da的基因产物。在本通讯中,我们报告该产物用[3H]甘油和[3H]棕榈酸标记,并且当用球蛋白(一种针对前脂蛋白信号肽酶的特异性抑制剂)处理细胞时,积累了分子量增加的前体分子。相同的前体分子由envC突变基因编码,其中EnvC氨基末端区域五肽序列Leu-Ile-Ala-Gly-Cys24中的半胱氨酸残基被色氨酸(Trp24)取代。该蛋白质未用[3H]甘油标记。结果表明,envC基因产物代表大肠杆菌细胞质膜的一种新的脂蛋白。