Seluanov A, Bibi E
Department of Biochemistry, Weizmann Institute of Science, Rehovot 76100, Israel.
J Biol Chem. 1997 Jan 24;272(4):2053-5. doi: 10.1074/jbc.272.4.2053.
In mammalian cells, many secretory proteins are targeted to the endoplasmic reticulum co-translationally, by the signal recognition particle (SRP) and its receptor. In Escherichia coli, the targeting of secretory proteins to the inner membrane can be accomplished post-translationally. Unexpectedly, despite this variance, E. coli contains essential genes encoding Ffh and FtsY with a significant similarity to proteins of the eukaryotic SRP machinery. In this study, we investigated the possibility that the prokaryotic SRP-like machinery is involved in biogenesis of membrane proteins in E. coli. The data presented here demonstrate that the SRP-receptor homologue, FtsY, is indeed essential for expression of integral membrane proteins in E. coli, indicating that, in the case of this group of proteins, FtsY and the mammalian SRP receptor have similar functions.
在哺乳动物细胞中,许多分泌蛋白通过信号识别颗粒(SRP)及其受体共翻译靶向内质网。在大肠杆菌中,分泌蛋白靶向内膜可在翻译后完成。出乎意料的是,尽管存在这种差异,但大肠杆菌含有编码Ffh和FtsY的必需基因,它们与真核生物SRP机制的蛋白质具有显著相似性。在本研究中,我们研究了原核生物中类似SRP的机制参与大肠杆菌膜蛋白生物合成的可能性。此处给出的数据表明,SRP受体同源物FtsY确实是大肠杆菌中整合膜蛋白表达所必需的,这表明,对于这一组蛋白质而言,FtsY与哺乳动物SRP受体具有相似的功能。