Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ
Analysis of MinC reveals two independent domains involved in interaction with MinD and FtsZ
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DOI：
10.1128/jb.182.14.3965-3971.2000
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发表时间：
2000-07-01
影响因子：
3.2
通讯作者：
Lutkenhaus, J
中科院分区：
文献类型：
--
作者：
Hu, ZL;Lutkenhaus, J
在大肠杆菌中，FtsZ在中间细胞组装成Z环，而在极性位点的组装被min系统阻止。MinC是该系统的一个组成部分，是FtsZ组装的抑制剂，通过与MinDE相互作用定位在细胞内。在这项研究中，我们发现，MinC由两个功能结构域连接的一个短的接头。当与MalE融合时，N-末端结构域能够抑制细胞分裂并阻止体外FtsZ组装。C-末端结构域与MinD相互作用，并且在野生型细胞中作为MalE融合体表达破坏了min功能，导致小细胞表型。我们还发现，MinC是一个寡聚体，可能是一个二聚体。虽然C-末端结构域显然足以寡聚化，但N-末端结构域也促进寡聚化。这些结果表明，MinC由两个独立的功能域：N-末端结构域能够抑制FtsZ组装和C-末端结构域负责本地化的MinC通过与MinD相互作用。这两个独立的结构域的融合是实现Z环组装的拓扑调控所必需的。
In Escherichia coli FtsZ assembles into a Z ring at midcell while assembly at polar sites is prevented by the min system. MinC, a component of this system, is an inhibitor of FtsZ assembly that is positioned within the cell by interaction with MinDE. In this study we found that MinC consists of two functional domains connected by a short linker. When fused to MalE the N-terminal domain is able to inhibit cell division and prevent FtsZ assembly in vitro. The C-terminal domain interacts with MinD, and expression in wild-type cells as a MalE fusion disrupts min function, resulting in a minicell phenotype. We also find that MinC is an oligomer, probably a dimer. Although the C-terminal domain is clearly sufficient for oligomerization, the N-terminal domain also promotes oligomerization. These results demonstrate that MinC consists of two independently functioning domains: an N-terminal domain capable of inhibiting FtsZ assembly and a C-terminal domain responsible for localization of MinC through interaction with MinD. The fusion of these two independent domains is required to achieve topological regulation of Z ring assembly.