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The Escherichia coli membrane protein insertase YidC assists in the biogenesis of Penicillin Binding Proteins

机译：大肠杆菌膜蛋白插入酶YidC辅助青霉素结合蛋白的生物发生

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Membrane proteins need to be properly inserted and folded in the membrane in order to perform a range of activities that are essential for the survival of bacteria. The Sec translocon and the YidC insertase are responsible for the insertion of the majority of proteins into the cytoplasmic membrane. YidC can act in combination with the Sec translocon in the insertion and folding of membrane proteins. However, YidC also functions as an insertase independently of the Sec translocon for so-called YidC-only substrates. In addition, YidC can act as a foldase and promote the proper assembly of membrane protein complexes. Here, we investigate the effect of Escherichia coli YidC depletion on the assembly of Penicillin Binding Proteins (PBPs), that are involved in cell wall synthesis. YidC depletion does not affect the total amount of the specific cell division PBP3 (FtsI) in the membrane, but the amount of active PBP3, as assessed by substrate binding, is reduced two-fold. A similar reduction in the amount of active PBP2 was observed, while the levels of active PBP1A/1B and PBP5 were essentially similar. PBP1B and PBP3 disappeared from higher Mw bands upon YidC depletion, indicating that YidC might play a role in PBP complex formation. Taken together, our results suggest that the foldase activity of YidC can extend to the periplasmic domains of membrane proteins. IMPORTANCE: This work addresses the role of the membrane protein insertase YidC in the biogenesis of Penicillin Binding Proteins (PBPs). PBPs are proteins containing one transmembrane segment and a large periplasmic or extracellular domain, which are involved in peptidoglycan synthesis. We observe that in the absence of YidC, two critical PBPs are not correctly folded even though the total amount of protein in the membrane is not affected. Our findings extend the function of YidC as a foldase for membrane protein (complexes) to periplasmic domains of membrane proteins.
机译：膜蛋白需要正确插入并折叠在膜中，以执行一系列对于细菌生存至关重要的活动。 Sec translocon和YidC插入酶负责将大多数蛋白质插入细胞质膜。 YidC可以与Sec translocon一起作用于膜蛋白的插入和折叠。但是，对于所谓的仅YidC底物，YidC还可以独立于Sec translocon用作插入酶。另外，YidC可以充当折叠酶并促进膜蛋白复合物的正确组装。在这里，我们调查了大肠杆菌YidC耗竭对参与细胞壁合成的青霉素结合蛋白（PBPs）组装的影响。 YidC消耗不会影响膜中特定细胞分裂PBP3（FtsI）的总量，但通过底物结合评估，活性PBP3的量减少了两倍。观察到活性PBP2量的减少类似，而活性PBP1A / 1B和PBP5的水平基本相似。在YidC耗尽后，PBP1B和PBP3从较高的Mw谱带消失，表明YidC可能在PBP复合物的形成中起作用。两者合计，我们的结果表明，YidC的折叠酶活性可以扩展到膜蛋白的周质域。重要提示：这项工作解决了膜蛋白插入酶YidC在青霉素结合蛋白（PBPs）的生物发生中的作用。 PBP是包含一个跨膜段和一个大的周质或胞外域的蛋白质，它们参与肽聚糖的合成。我们观察到，在没有YidC的情况下，即使膜中的蛋白质总量不受影响，两个关键的PBP也无法正确折叠。我们的发现将YidC的功能扩展为膜蛋白（复合体）的折叠酶，直至膜蛋白的周质结构域。

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