A Diguanylate Cyclase Acts as a Cell Division Inhibitor in a Two-Step Response to Reductive and Envelope Stresses.
A Diguanylate Cyclase Acts as a Cell Division Inhibitor in a Two-Step Response to Reductive and Envelope Stresses.
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在对还原和包膜应力的两步响应中，二烷基酸酯环化酶充当细胞分裂抑制剂。
DOI：
10.1128/mbio.00822-16
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发表时间：
2016-08-09
期刊：
影响因子：
6.4
通讯作者：
Harshey RM
中科院分区：
文献类型：
--
作者：
Kim HK;Harshey RM
细胞分裂停滞是一个普遍的检查点，以应对产生细胞应激的环境攻击。在细菌中，环二-GMP（c-di-GMP）信号传导网络是响应于细胞外/细胞内刺激而调节关键过程的几种信号转导系统之一。在这里，我们发现，二鸟苷酸环化酶YfiN作为一个双功能蛋白，产生c-di-GMP在还原应力的反应，然后动态重新定位到分裂位点，以阻止细胞分裂在大肠杆菌中的信封应力。YfN通过与早期分裂蛋白相互作用定位于Z环，并通过阻止间隔肽聚糖合成的起始来阻止细胞分裂。这些研究揭示了二鸟苷酸环化酶在响应环境变化中的新作用，以及阻止细胞分裂的新机制。虽然c-di-GMP信号传导的主要作用是控制自由移动或定居在生物膜中的决定，但最近的研究显示c-di-GMP信号传导的输出功能范围更广。这项工作报告了YfiN的意想不到的第二个作用，YfiN是革兰氏阴性细菌中的保守二鸟苷酸环化酶，已知有助于在宿主中的持久性。我们发现，YfIN作为细胞分裂抑制剂响应于包膜应激。与已知的细胞分裂抑制剂不同，YfiN与细胞分裂蛋白的相互作用保留了中细胞处的Z环，但防止了隔膜内陷。YfiN的新功能不仅强调了c-di-GMP信号传导的多功能性，而且描述了细胞分裂检查点的新机制。
Cell division arrest is a universal checkpoint in response to environmental assaults that generate cellular stress. In bacteria, the cyclic di-GMP (c-di-GMP) signaling network is one of several signal transduction systems that regulate key processes in response to extra-/intracellular stimuli. Here, we find that the diguanylate cyclase YfiN acts as a bifunctional protein that produces c-di-GMP in response to reductive stress and then dynamically relocates to the division site to arrest cell division in response to envelope stress in Escherichia coli. YfiN localizes to the Z ring by interacting with early division proteins and stalls cell division by preventing the initiation of septal peptidoglycan synthesis. These studies reveal a new role for a diguanylate cyclase in responding to environmental change, as well as a novel mechanism for arresting cell division. While the major role of c-di-GMP signaling is to control the decision to move freely or settle in a biofilm, recent studies show a broader range of output functions for c-di-GMP signaling. This work reports an unexpected second role for YfiN, a conserved diguanylate cyclase in Gram-negative bacteria, known to contribute to persistence in the host. We find that YfiN acts as a cell division inhibitor in response to envelope stress. Unlike known cell division inhibitors, the interaction of YfiN with cell division proteins retains the Z ring at the midcell but prevents septal invagination. The new function of YfiN not only emphasizes the versatility of c-di-GMP signaling but describes a novel mechanism for a cell division checkpoint.