A Novel Z-Ring Associated Protein ZapA-Like Protein (PA5407) From Pseudomonas aeruginosa Promotes FtsZ to Form Double Filaments.
A Novel Z-Ring Associated Protein ZapA-Like Protein (PA5407) From Pseudomonas aeruginosa Promotes FtsZ to Form Double Filaments.
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铜绿假单胞菌的一种新型Z-RING蛋白ZAPA样蛋白（PA5407）促进FTSZ形成双丝丝。
DOI：
10.3389/fmicb.2021.717013
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发表时间：
2021
影响因子：
5.2
通讯作者：
Chen Y
中科院分区：
文献类型：
--
作者：
Wang X;Ma X;Li Z;Niu M;Zhai M;Chen Y
细菌细胞分裂是由收缩环（Z环）的组装启动的，收缩环由自组装的FtsZ原丝和数十种其他相关蛋白组成。ZapA是几乎所有细菌中发现的一种调节蛋白，它稳定FtsZ原丝以形成束并增强Z环缩合。本文报道了铜绿假单胞菌的另一种小分子蛋白ZapA-Like protein（ZapAL; PA 5407），是一种新的FtsZ相关蛋白。ZapAL存在于许多假单胞菌属物种中，与ZapA仅具有20%的序列同一性。ZapAL与FtsZ相互作用并诱导FtsZ形成长直双丝;相比之下，ZapA促进具有多个FtsZ丝的长束。ZapAL对FtsZ的GTdR活性仅有轻微影响，当溶液中加入10 μM ZapAL时，FtsZ的GTdR活性降低约26%。然而，用光散射法研究它们的组装动力学，我们发现FtsZ-ZapAL双丝是稳定的，没有观察到解聚过程，这与ZapA不同。进一步的研究发现ZapA和ZapL可能形成异二聚体。FtsZ-ZapA-ZapAL混合物形成的纤维束在GTP水解后脱粘。与ZapAL与FtsZ的体外相互作用一致，观察到ZapAL-GFP的表达为细胞中间的窄带或斑点，表明其是细菌分裂机制的组分。与ZapA类似，ZapAL也不是细菌细胞分裂所必需的。当zapAL基因缺失或在正常条件下过表达时，观察到的变化很小;然而，ZapAL的过表达导致zapA缺陷细胞生长约2倍长，显示出轻微的细菌分裂缺陷。虽然我们还不清楚ZapAL的确切生理作用，但我们的研究结果表明，ZapAL是一种新的Z环相关蛋白，它可能与ZapA一起稳定FtsZ原丝和Z环结构。
Bacterial cell division is initiated by the assembly of the contraction ring (Z-ring), which consists of the self-assembled FtsZ protofilaments and dozens of other associate proteins. ZapA, a regulatory protein found in almost all bacteria, stabilizes FtsZ protofilaments to form bundles and enhances the Z-ring condensation. Here, we reported that another small protein from Pseudomonas aeruginosa, ZapA-Like protein (ZapAL; PA5407), is a new FtsZ associated protein. ZapAL exists in many Pseudomonas species and shares only 20% sequence identity to ZapA. ZapAL interacts with FtsZ and induces FtsZ to form long straight double filaments; in comparison, ZapA promotes long bundles with multiple FtsZ filaments. ZapAL has only a mild effect on GTPase activity of FtsZ, which is reduced by around 26% when 10 μM ZapAL is added in the solution. However, to study their assembly dynamics using light-scattering assay, we found that FtsZ-ZapAL double filament is stable and no depolymerization process is observed, which is different from ZapA. Further research found that ZapA and ZapL are likely to form heterodimers. The bundles formed by the mixture of FtsZ-ZapA-ZapAL will depolymerize after GTP is hydrolyzed. Consistent with ZapAL interaction with FtsZ in vitro, the expression of ZapAL-GFP was observed as a narrow band or spots in the middle of the cells, suggesting that it is a component of bacterial division machinery. Similar to ZapA, ZapAL is also not essential for bacterial cell division. Little changes were observed when zapAL gene was deleted, or overexpressed under normal conditions; however, overexpression of ZapAL caused zapA-deficient cells to grow approximately two times longer, showing a mild bacterial division defect. Although we still do not know the exact physiological roles of ZapAL, our results suggest that ZapAL is a novel Z-ring associate protein, which may work together with ZapA to stabilize the FtsZ protofilament and Z-ring structure.
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DOI：
10.1038/nrmicro.2016.26
发表时间：
2016-04
期刊：
Nature reviews. Microbiology
影响因子：
--
作者：
Haeusser DP;Margolin W
通讯作者：
Margolin W
影响因子：
7.5
作者：
Barrows JM;Goley ED
通讯作者：
Goley ED
影响因子：
2.9
作者：
Chen, Yaodong;Erickson, Harold P.
通讯作者：
Erickson, Harold P.
影响因子：
4.1
作者：
Pacheco-Gomez, Raul;Cheng, Xi;Dafforn, Timothy R.
通讯作者：
Dafforn, Timothy R.
影响因子：
3.2
作者：
Hale, Cynthia A.;Shiomi, Daisuke;de Boer, Piet A. J.
通讯作者：
de Boer, Piet A. J.