The C-terminal domain of MinC, a cell division regulation protein, is sufficient to form a copolymer with MinD
The C-terminal domain of MinC, a cell division regulation protein, is sufficient to form a copolymer with MinD
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DOI：
10.1111/febs.16890
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发表时间：
2023-06-25
期刊：
影响因子：
5.4
通讯作者：
Chen，Yaodong
中科院分区：
文献类型：
--
作者：
Wang，Na;Sun，Haiyu;Chen，Yaodong
Assembly of cell division protein FtsZ into the Z‐ring at the division site is a key step in bacterial cell division. The Min proteins can restrict the Z‐ring to the middle of the cell. MinC is the main protein that obstructs Z‐ring formation by inhibiting FtsZ assembly. Its N‐terminal domain (MinCN) regulates the localization of the Z‐ring by inhibiting FtsZ polymerization, while its C‐terminal domain (MinCC) binds to MinD as well as to FtsZ. Previous studies have shown that MinC and MinD form copolymersin vitro. This copolymer may greatly enhance the binding of MinC to FtsZ, and/or prevent FtsZ filaments from diffusing to the ends of the cell. Here, we investigated the assembly properties of MinCC–MinD ofPseudomonas aeruginosa. We found that MinCCis sufficient to form the copolymers. Although MinCC–MinD assembles into larger bundles, most likely because MinCCis spatially more readily bound to MinD, its copolymerization has similar dynamic properties: the concentration of MinD dominates their copolymerization. The critical concentration of MinD is around 3 μmand when MinD concentration is high enough, a low concentration MinCCcould still be copolymerized. We also found that MinCC–MinD can still rapidly bind to FtsZ protofilaments, providing direct evidence that MinCCalso interacts directly with FtsZ. However, although the presence ofminCCcan slightly improve the division defect ofminC‐knockout strains and shorten the cell length from an average of 12.2 ± 6.7 to 6.6 ± 3.6 μm, it is still insufficient for the normal growth and division of bacteria.
