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首页> 美国卫生研究院文献>Journal of Bacteriology >Insertion of a MalE β-Galactosidase Fusion Protein into the Envelope of Escherichia coli Disrupts Biogenesis of Outer Membrane Proteins and Processing of Inner Membrane Proteins
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Insertion of a MalE β-Galactosidase Fusion Protein into the Envelope of Escherichia coli Disrupts Biogenesis of Outer Membrane Proteins and Processing of Inner Membrane Proteins

机译：将MalEβ-半乳糖苷酶融合蛋白插入到大肠杆菌的包膜中会破坏外膜蛋白的生物发生和内膜蛋白的加工。

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摘要

The synthesis of a membrane-bound MalE β-galactosidase hybrid protein, when induced by growth of Escherichia coli on maltose, leads to inhibition of cell division and eventually a reduced rate of mass increase. In addition, the relative rate of synthesis of outer membrane proteins, but not that of inner membrane proteins, was reduced by about 50%. Kinetic experiments demonstrated that this reduction coincided with the period of maximum synthesis of the hybrid protein (and another maltose-inducible protein, LamB). The accumulation of this abnormal protein in the envelope therefore appeared specifically to inhibit the synthesis, the assembly of outer membrane proteins, or both, indicating that the hybrid protein blocks some export site or causes the sequestration of some limiting factor(s) involved in the export process. Since the MalE protein is normally located in the periplasm, the results also suggest that the synthesis of periplasmic and outer membrane proteins may involve some steps in common. The reduced rate of synthesis of outer membrane proteins was also accompanied by the accumulation in the envelope of at least one outer membrane protein and at least two inner membrane proteins as higher-molecular-weight forms, indicating that processing (removal of the N-terminal signal sequence) was also disrupted by the presence of the hybrid protein. These results may indicate that the assembly of these membrane proteins is blocked at a relatively late step rather than at the level of primary recognition of some site by the signal sequence. In addition, the results suggest that some step common to the biogenesis of quite different kinds of envelope protein is blocked by the presence of the hybrid protein.
机译：当大肠杆菌在麦芽糖上的生长诱导时，膜结合的MalEβ-半乳糖苷酶杂合蛋白的合成会导致细胞分裂受到抑制，并最终导致质量增加速率降低。另外，外膜蛋白的相对合成速率降低了约50％，而内膜蛋白的相对合成速率降低了约50％。动力学实验表明，这种降低与杂合蛋白（和另一种麦芽糖诱导蛋白LamB）的最大合成时间相吻合。因此，这种异常蛋白在包膜中的积聚似乎特别抑制了合成，外膜蛋白的组装或同时抑制了两者，这表明杂合蛋白会阻断某些输出位点或引起与该蛋白相关的某些限制因子的隔离。导出过程。由于MalE蛋白通常位于周质中，因此结果还表明周质和外膜蛋白的合成可能涉及一些共同的步骤。外膜蛋白合成速率的降低还伴随着至少一种外膜蛋白和至少两种内膜蛋白以较高分子量形式在包膜中的积累，表明加工（去除了N-末端信号序列）也因杂合蛋白的存在而被破坏。这些结果可能表明这些膜蛋白的组装在相对较晚的步骤被阻断，而不是在信号序列对某些位点的主要识别水平上被阻断。另外，结果表明杂合蛋白的存在阻止了完全不同种类的包膜蛋白的生物发生中共有的某些步骤。

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