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首页> 外文期刊>PLoS Genetics >NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli
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NlpD links cell wall remodeling and outer membrane invagination during cytokinesis in Escherichia coli

机译：NlpD在大肠杆菌胞质分裂过程中联系细胞壁重塑和外膜内陷

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Cytokinesis in gram-negative bacteria requires the constriction of all three cell envelope layers: the inner membrane (IM), the peptidoglycan (PG) cell wall and the outer membrane (OM). In order to avoid potentially lethal breaches in cell integrity, this dramatic reshaping of the cell surface requires tight coordination of the different envelope remodeling activities of the cytokinetic ring. However, the mechanisms responsible for this coordination remain poorly defined. One of the few characterized regulatory points in the envelope remodeling process is the activation of cell wall hydrolytic enzymes called amidases. These enzymes split cell wall material shared by developing daughter cells to facilitate their eventual separation. In Escherichia coli, amidase activity requires stimulation by one of two partially redundant activators: EnvC, which is associated with the IM, and NlpD, a lipoprotein anchored in the OM. Here, we investigate the regulation of amidase activation by NlpD. Structure-function analysis revealed that the OM localization of NlpD is critical for regulating its amidase activation activity. To identify additional factors involved in the NlpD cell separation pathway, we also developed a genetic screen using a flow cytometry-based enrichment procedure. This strategy allowed us to isolate mutants that form long chains of unseparated cells specifically when the redundant EnvC pathway is inactivated. The screen implicated the Tol-Pal system and YraP in NlpD activation. The Tol-Pal system is thought to promote OM invagination at the division site. YraP is a conserved protein of unknown function that we have identified as a new OM-localized component of the cytokinetic ring. Overall, our results support a model in which OM and PG remodeling events at the division site are coordinated in part through the coupling of NlpD activation with OM invagination.
机译：革兰氏阴性细菌的胞质分裂需要收缩所有三个细胞包膜层：内膜（IM），肽聚糖（PG）细胞壁和外膜（OM）。为了避免潜在的致命的细胞完整性破坏，细胞表面的这种显着重塑需要细胞动力学环的不同包膜重塑活性的紧密协调。但是，负责这种协调的机制仍然定义不清。包膜重塑过程中为数不多的调节点之一是称为酰胺酶的细胞壁水解酶的激活。这些酶分裂发育中的子细胞共享的细胞壁物质，以促进其最终分离。在大肠杆菌中，酰胺酶活性需要两个部分冗余的激活剂之一刺激：EnvC（与IM相关）和NlpD（锚定在OM中的脂蛋白）。在这里，我们调查NlpD酰胺酶激活的调节。结构功能分析表明，NlpD的OM定位对于调节其酰胺酶激活活性至关重要。为了确定涉及NlpD细胞分离途径的其他因素，我们还使用基于流式细胞仪的富集程序开发了基因筛选。这种策略使我们能够分离出形成未分离细胞长链的突变体，特别是在冗余EnvC途径失活时。屏幕暗示了Tol-Pal系统和YraP参与了NlpD激活。 Tol-Pal系统被认为可促进分裂部位的OM内陷。 YraP是一种功能未知的保守蛋白，我们已将其鉴定为细胞动力学环的一个新的OM定位组件。总体而言，我们的结果支持一个模型，其中分裂部位的OM和PG重塑事件通过NlpD激活与OM内陷的结合而部分协调。

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