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Membrane Targeting and Insertion of the C-Tail Protein SciP

机译:膜靶向和C尾蛋白SciP的插入

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C-tailed membrane proteins insert into the bilayer post-translationally because the hydrophobic anchor segment leaves the ribosome at the end of translation. Nevertheless, we find here evidence that the targeting of SciP to the membrane of Escherichia coli occurs co-translationally since signal elements in the N-terminal part of the SciP protein sequence are present. Two short hydrophobic sequences were identified that targeted a green fluorescent protein-SciP fusion protein to the membrane involving the signal recognition particle. After targeting, the membrane insertion of SciP is catalyzed by YidC independent of the SecYEG translocase. However, when the C-terminal tail of SciP was extended to 21 as residues, we found that SecYEG becomes involved and makes its membrane insertion more efficient. (C) 2016 Elsevier Ltd. All rights reserved.
机译:C尾膜蛋白在翻译后插入双层中,因为疏水锚段在翻译结束时离开了核糖体。然而,我们在这里发现证据表明,由于SciP蛋白序列N端部分存在信号元件,因此SciP靶向大肠杆菌膜是共翻译发生的。鉴定了两个短的疏水序列,其将绿色荧光蛋白-SciP融合蛋白靶向涉及信号识别颗粒的膜。靶向后,独立于SecYEG易位酶的YidC催化SciP的膜插入。然而,当SciP的C末端尾巴延伸至21作为残基时,我们发现SecYEG参与其中并使其膜插入更加有效。 (C)2016 Elsevier Ltd.保留所有权利。

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