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Association of Escherichia coli ribosomes with the inner membrane requires the signal recognition particle receptor but is independent of the signal recognition particle

机译:大肠杆菌核糖体与内膜的结合需要信号识别颗粒受体,但与信号识别颗粒无关

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摘要

In mammalian cells, as well as Escherichia coli ribosomes translat- ing membrane proteins interact cotranslationally with translocons in the membrane, and this interaction is essential for proper insertion of nascent polypeptides into the membrane. Both the signal recognition particle (SRP) and its receptor (SR) are required for functional association of ribosomes translating integral mem- hrane proteins with the translocon. Herein, we confirm that mem- hrane targeting of E. coli ribosomes requires the prokaryotic SRα homolog FtsY in vivo. Surprisingly, however, depletion of the E coli SRP54 homolog (Ffh) has no significant effect on binding of ribosomes to the membrane. although Ffh depletion is detrimental to growth. These and other observations suggest that, in E. coli, SRP may operate downstream of SR-mediated targeting of ribo- somes to the plasma membrane.
机译:在哺乳动物细胞以及大肠杆菌核糖体翻译膜蛋白中,它们与膜中的转座子共翻译相互作用,这种相互作用对于将新生多肽正确插入膜中至关重要。信号识别颗粒(SRP)及其受体(SR)都是核糖体将整合的膜蛋白与反式转运子进行功能结合所必需的。在本文中,我们确认以膜状靶向大肠杆菌核糖体在体内需要原核SRα同源物FtsY。然而,令人惊讶的是,大肠杆菌SRP54同源物(Ffh)的消耗对核糖体与膜的结合没有显着影响。尽管Ffh耗竭不利于增长。这些和其他观察结果表明,在大肠杆菌中,SRP可能在SR介导的核糖体靶向质膜的下游运行。

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