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首页> 外文期刊>Journal of bacteriology >Multiple Interactions between Pullulanase Secreton Components Involved in Stabilization and Cytoplasmic Membrane Association of PulE
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Multiple Interactions between Pullulanase Secreton Components Involved in Stabilization and Cytoplasmic Membrane Association of PulE

机译：参与稳定化的支链淀粉酶分泌成分与PulE的细胞质膜缔合之间的多重相互作用

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摘要

We report attempts to analyze interactions between components of the pullulanase (Pul) secreton (type II secretion machinery) fromKlebsiella oxytoca encoded by a multiple-copy-number plasmid in Escherichia coli. Three of the 15 Pul proteins (B, H, and N) were found to be dispensable for pullulanase secretion. The following evidence leads us to propose that PulE, PulL, and PulM form a subcomplex with which PulC and PulG interact. The integral cytoplasmic membrane protein PulL prevented proteolysis and/or aggregation of PulE and mediated its association with the cytoplasmic membrane. The cytoplasmic, N-terminal domain of PulL interacted directly with PulE, and both PulC and PulM were required to prevent proteolysis of PulL. PulM and PulL could be cross-linked as a heterodimer whose formation in a strain producing the secreton required PulG. However, PulL and PulM produced alone could also be cross-linked in a 52-kDa complex, indicating that the secreton exerts subtle effects on the interaction between PulE and PulL. Antibodies against PulM coimmunoprecipitated PulL, PulC, and PulE from detergent-solubilized cell extracts, confirming the existence of a complex containing these four proteins. Overproduction of PulG, which blocks secretion, drastically reduced the cellular levels of PulC, PulE, PulL, and PulM as well as PulD (secretin), which probably interacts with PulC. The Pul secreton components E, F, G, I, J, K, L, and M could all be replaced by the corresponding components of the Out secretons of Erwinia chrysanthemi and Erwinia carotovora, showing that they do not play a role in secretory protein recognition and secretion specificity.
机译：我们报告尝试分析大肠杆菌中由多拷贝数质粒编码的产酸克雷伯菌的支链淀粉酶（Pul）分泌蛋白（II型分泌机制）之间的相互作用。发现15个Pul蛋白中的三个（B，H和N）对于支链淀粉酶的分泌是不可缺少的。以下证据使我们建议，PulE，PulL和PulM形成PulC和PulG相互作用的亚复合物。完整的细胞质膜蛋白PulL阻止了PulE的蛋白水解和/或聚集，并介导了其与细胞质膜的缔合。 PulL的胞质N末端结构域直接与PulE相互作用，同时需要PulC和PulM来阻止PulL的蛋白水解。 PulM和PulL可以作为异二聚体进行交联，其异质二聚体在产生分泌素的菌株中形成所需的PulG。但是，单独生产的PulL和PulM也可以在52 kDa的复合物中交联，表明该分泌物对PulE和PulL之间的相互作用产生微妙的影响。抗PulM的抗体可从去污剂溶解的细胞提取物中共免疫沉淀PulL，PulC和PulE，从而证实了含有这四种蛋白质的复合物的存在。阻止分泌的PulG的过量生产，大大降低了PulC，PulE，PulL和PulM以及可能与PulC相互作用的PulD（分泌素）的细胞水平。 Pul分泌物成分E，F，G，I，J，K，L和M均可被和 Erwinia carotovora 的Out分泌物的相应成分取代。 em>，表明它们在分泌蛋白识别和分泌特异性中不起作用。

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