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The mechanosensitive channel protein MscL is targeted by the SRP to the novel YidC membrane insertion pathway of Escherichia coli

机译:机械敏感通道蛋白MscL被SRP靶向大肠杆菌的新型YidC膜插入途径

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The mechanosensitive channel MscL in the inner membrane of Escherichia coli is a homopentameric complex involved in homeostasis when cells are exposed to hypo-osmotic conditions. The E. coli MscL, protein is synthesized as a polypeptide of 136 amino acid residues and uses the bacterial signal recognition particle (SRP) for membrane targeting. The protein is inserted into the membrane independently of the Sec translocon. Mutants affected in the Sec-components are competent for MscL assembly. Translocation of the periplasmic domain was detected using a membrane-impermeant, sulfhydryl-specific gel-shift reagent. The modification of a single cysteine residue at position 68 indicated its translocation across the inner membrane. From these in vivo experiments, it is concluded that the electrical chemical membrane potential is not necessary for membrane insertion of MscL. However, depletion of the membrane insertase YidC inhibits translocation of the protein across the membrane. We show here that YidC is essential for efficient membrane insertion of the MscL protein. YidC is a component of a recently identified membrane insertion pathway that is evolutionarily conserved in bacteria, mitochondria and chloroplasts. (c) 2006 Elsevier Ltd. All rights reserved.
机译:当细胞暴露于低渗条件时,大肠杆菌内膜中的机械敏感通道MscL是参与稳态的同五聚体复合物。大肠杆菌MscL蛋白合成为具有136个氨基酸残基的多肽,并使用细菌信号识别颗粒(SRP)进行膜靶向。蛋白质独立于Sec translocon插入膜中。受Sec组件影响的突变体可以胜任MscL组装。使用不透膜的巯基特异性凝胶转移试剂检测周质结构域的移位。第68位的单个半胱氨酸残基的修饰表明其跨内膜易位。从这些体内实验得出结论,电化学膜电势对于MscL的膜插入不是必需的。但是,膜插入酶YidC的耗竭抑制了蛋白质跨膜的转运。我们在这里显示,YidC对于有效膜插入MscL蛋白至关重要。 YidC是最近鉴定的膜插入途径的组成部分,该途径在细菌,线粒体和叶绿体中在进化上是保守的。 (c)2006 Elsevier Ltd.保留所有权利。

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