FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
FtsZ collaborates with penicillin binding proteins to generate bacterial cell shape in Escherichia coli
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DOI：
10.1128/jb.186.20.6768-6774.2004
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发表时间：
2004-10-01
影响因子：
3.2
通讯作者：
Young, KD
中科院分区：
文献类型：
--
作者：
Varma, A;Young, KD
细菌采用和保持个体形状的机制仍然是个谜。悬而未决的问题包括为什么细胞具有一定的大小、长度和宽度;为什么它们是均匀的或不规则的;为什么有些分支，而另一些则没有。以前，我们表明，大肠杆菌突变体缺乏多种青霉素结合蛋白（PBPs）显示出广泛的形态多样性。由于这些细胞中的缺陷位点表现出不适当定位的极点的结构和功能特征，我们研究了细胞分裂和形状之间的联系。在这里，我们表明，在半许可条件下，温度敏感的FtsZ 84蛋白产生分支和异常细胞在一个高频率的突变体缺乏PBP 5，这种表型是加剧了额外的肽聚糖内肽酶的损失。令人惊讶的是，某些ftsZ 84菌株在非允许温度下裂解而不是裂解，并且野生型FtsZ的抑制迫使一些突变体形成紧密缠绕的类肉瘤形态。结果表明，细菌形状的重要方面是由一个以前未认识到的分隔机械和表面上轻微的肽聚糖修饰酶之间的关系，并在某些情况下，不适当的FtsZ功能可以破坏细胞的结构完整性。
The mechanisms by which bacteria adopt and maintain individual shapes remain enigmatic. Outstanding questions include why cells are a certain size, length, and width; why they are uniform or irregular; and why some branch while others do not. Previously, we showed that Escherichia coli mutants lacking multiple penicillin binding proteins (PBPs) display extensive morphological diversity. Because defective sites in these cells exhibit the structural and functional characteristics of improperly localized poles, we investigated the connection between cell division and shape. Here we show that under semipermissive conditions the temperature-sensitive FtsZ84 protein produces branched and aberrant cells at a high frequency in mutants lacking PBP 5, and this phenotype is exacerbated by the loss of additional peptidoglycan endopeptidases. Surprisingly, certain ftsZ84 strains lyse at the nonpermissive temperature instead of filamenting, and inhibition of wild-type FtsZ forces some mutants into tightly wound spirillum-like morphologies. The results demonstrate that significant aspects of bacterial shape are dictated by a previously unrecognized relationship between the septation machinery and ostensibly minor peptidoglycan-modifying enzymes and that under certain circumstances improper FtsZ function can destroy the structural integrity of the cell.