FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.
FtsA reshapes membrane architecture and remodels the Z-ring in Escherichia coli.
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DOI：
10.1111/mmi.13902
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发表时间：
2018-03
影响因子：
3.6
通讯作者：
Camberg JL
中科院分区：
文献类型：
--
作者：
Conti J;Viola MG;Camberg JL
原核生物的细胞分裂始于中间细胞的z环组装，在大肠杆菌中，z环通过与FtsA（一种广泛保守的肌动蛋白同源物）的直接相互作用被拴在细胞质膜的内小叶上。z形环由类微管蛋白的FtsZ聚合物组成，并被认为提供收缩力。在这里，我们证明了FtsA对膜施加力，导致膜结构的重新分配，稳定地水解ATP，并直接在重构系统中参与FtsZ聚合物。FtsA通过将c端膜靶向序列（MTS）插入双分子层介导磷脂重组，并通过传递给MTS的核苷酸依赖性构象变化进一步促进磷脂重组。FtsA还通过与FtsZ c端直接相互作用将FtsZ招募到磷脂囊泡中，并调节FtsZ组装动力学。这些结果暗示了肌动蛋白同源物FtsA在建立z环支架的同时直接重塑膜，并为分裂开始时局部细胞壁重塑、内陷和收缩提供了机制见解。FtsA是一种参与细菌细胞分裂的肌动蛋白样ATP酶，它与磷脂囊泡结合，将c端插入磷脂双分子层，并在ATP存在下迅速重新配置囊泡结构。在体外将FtsZ聚合物募集到FtsA蛋白脂质体上，建立了一个大的支架。我们的研究结果表明，在分裂过程中，FtsA在膜表面聚合并对膜施加力，导致z环处的局部膜重组和细胞壁重塑。
Cell division in prokaryotes initiates with assembly of the Z-ring at midcell, which, in Escherichia coli, is tethered to the inner leaflet of the cytoplasmic membrane through a direct interaction with FtsA, a widely conserved actin homolog. The Z-ring is comprised of polymers of tubulin-like FtsZ and has been suggested to provide the force for constriction. Here, we demonstrate that FtsA exerts force on membranes causing redistribution of membrane architecture, robustly hydrolyzes ATP and directly engages FtsZ polymers in a reconstituted system. Phospholipid reorganization by FtsA occurs rapidly and is mediated by insertion of a C-terminal membrane targeting sequence (MTS) into the bilayer and further promoted by a nucleotide-dependent conformational change relayed to the MTS. FtsA also recruits FtsZ to phospholipid vesicles via a direct interaction with the FtsZ C-terminus and regulates FtsZ assembly kinetics. These results implicate the actin homolog FtsA in establishment of a Z-ring scaffold, while directly remodeling the membrane, and provide mechanistic insight into localized cell wall remodeling, invagination and constriction at the onset of division. Abbreviated Summary FtsA is an actin-like ATPase involved in bacterial cell division that binds to phospholipid vesicles, inserts the C-terminus into the phospholipid bilayer and rapidly reconfigures vesicle architecture in the presence of ATP. Recruitment of FtsZ polymers to the FtsA proteo-liposomes in vitro establishes a large scaffold. Our results suggest that during division, FtsA polymerizes at the membrane surface and exerts force on membrane, leading to localized membrane reorganization and cell wall remodeling at the Z-ring.
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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：
64.8
作者：
Ford, MGJ;Mills, IG;McMahon, HT
通讯作者：
McMahon, HT
影响因子：
3.2
作者：
GAYDA, RC;HENK, MC;LEONG, D
通讯作者：
LEONG, D
影响因子：
3.6
作者：
Aarsman, MEG;Piette, A;den Blaauwen, T
通讯作者：
den Blaauwen, T
影响因子：
3.6
作者：
Bernard, Christophe S.;Sadasivam, Mahalakshmi;Margolin, William
通讯作者：
Margolin, William