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首页> 外文期刊>Journal of Molecular Biology >A tag at the carboxy terminus prevents membrane integration of VDAC1 in mammalian mitochondria.
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A tag at the carboxy terminus prevents membrane integration of VDAC1 in mammalian mitochondria.

机译：羧基末端的标签可防止VDAC1在哺乳动物线粒体中发生膜整合。

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摘要

beta-Barrel proteins are found in the outer membranes of bacteria, chloroplasts and mitochondria. The evolutionary conserved sorting and assembly machinery (SAM complex) assembles mitochondrial beta-barrel proteins, such as voltage-dependent anion-selective channel 1 (VDAC1), into complexes in the outer membrane by recognizing a sorting beta-signal in the carboxy-terminal part of the protein. Here we show that in mammalian mitochondria, masking of the C-terminus of beta-barrel proteins by a tag leads to accumulation of soluble misassembled protein in the intermembrane space, which causes mitochondrial fragmentation and loss of membrane potential. A similar phenotype is observed if the beta-signal is shortened, removed or when the conserved hydrophobic residues in the beta-signal are mutated. The length of the tag at the C-terminus is critical for the assembly of VDAC1, as well as the amino acid residues at positions 130, 222, 225 and 251 of the protein. We propose that if the recognition of the beta-signal or the folding of the beta-barrel proteins is inhibited, the nonassembled protein will accumulate in the intermembrane space, aggregate and damage mitochondria. This effect offers easy tools for studying the requirements for the membrane assembly of beta-barrel proteins, but also advises caution when interpreting the outcome of the beta-barrel protein overexpression experiments.
机译：β-桶蛋白存在于细菌，叶绿体和线粒体的外膜中。进化的保守分选和组装机制（SAM复合物）通过识别羧基末端的分选β信号，将线粒体β桶蛋白（如电压依赖性阴离子选择通道1（VDAC1））组装成外膜中的复合物。部分蛋白质。在这里，我们显示在哺乳动物的线粒体中，标签对β-桶蛋白的C端的掩盖导致膜间空间中可溶性错配蛋白的积累，从而导致线粒体破碎和膜电位下降。如果β信号被缩短，去除或当β信号中的保守疏水残基发生突变时，观察到相似的表型。标签在C端的长度对于VDAC1的组装以及蛋白质130、222、225和251位的氨基酸残基的组装至关重要。我们建议，如果抑制了对β信号的识别或β桶蛋白的折叠，则未组装的蛋白将在膜间空间积聚，聚集并破坏线粒体。这种效应为研究β-桶蛋白的膜组装要求提供了简便的工具，但在解释β-桶蛋白过表达实验的结果时也建议谨慎。

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