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Escherichia coli SRP Its Protein Subunit Ffh and the Ffh M Domain Are Able To Selectively Limit Membrane Protein Expression When Overexpressed

机译:大肠杆菌SRP其蛋白亚基Ffh和Ffh M结构域能够选择性地过表达时限制膜蛋白的表达。

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摘要

The Escherichia coli signal recognition particle (SRP) system plays an important role in membrane protein biogenesis. Previous studies have suggested indirectly that in addition to its role during the targeting of ribosomes translating membrane proteins to translocons, the SRP might also have a quality control role in preventing premature synthesis of membrane proteins in the cytoplasm. This proposal was studied here using cells simultaneously overexpressing various membrane proteins and either SRP, the SRP protein Ffh, its 4.5S RNA, or the Ffh M domain. The results show that SRP, Ffh, and the M domain are all able to selectively inhibit the expression of membrane proteins. We observed no apparent changes in the steady-state mRNA levels or membrane protein stability, suggesting that inhibition may occur at the level of translation, possibly through the interaction between Ffh and ribosome-hydrophobic nascent chain complexes. Since E. coli SRP does not have a eukaryote-like translation arrest domain, we discuss other possible mechanisms by which this SRP might regulate membrane protein translation when overexpressed.
机译:大肠杆菌信号识别颗粒(SRP)系统在膜蛋白生物发生中起重要作用。先前的研究间接表明,除了在核糖体靶向中将膜蛋白翻译为转座子的过程中,SRP可能还具有防止细胞膜蛋白过早合成的质量控制作用。本文使用同时表达各种膜蛋白和SRP,SRP蛋白Ffh,其4.5S RNA或Ffh M结构域的细胞研究了该建议。结果表明,SRP,Ffh和M结构域均能够选择性抑制膜蛋白的表达。我们观察到稳态mRNA水平或膜蛋白稳定性没有明显变化,表明抑制可能发生在翻译水平,可能是通过Ffh与核糖体-疏水性新生链复合物之间的相互作用引起的。由于大肠杆菌SRP没有真核生物样的翻译阻滞域,因此我们讨论了其他SRP在过表达时可能调节膜蛋白翻译的可能机制。

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