The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm
The cell envelope stress response mediated by the LiaFSRLm three-component system of Listeria monocytogenes is controlled via the phosphatase activity of the bifunctional histidine kinase LiaSLm
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DOI：
10.1099/mic.0.044776-0
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发表时间：
2011-02-01
期刊：
影响因子：
2.8
通讯作者：
Beier, Dagmar
中科院分区：
文献类型：
--
作者：
Fritsch, Frederike;Mauder, Norman;Beier, Dagmar
厚壁菌门的大多数成员都拥有双组分系统 (TCS) LiaSR，该系统参与对细胞膜应激的反应，尤其是由脂质 II 循环抑制剂引起的细胞膜应激。在所有详细研究的 LiaSR 系统中，LiaSR 介导的信号转导已被证明受到 liaSR 上游编码的膜蛋白 LiaF 的负控制。在本研究中，我们分析了单核细胞增生李斯特菌 (LiaSR(Lm)) 的 LiaSR 直系同源物。全基因组转录谱表明，在诱导刺激存在的情况下，LiaSR(Lm) 的激活通过膜相关蛋白和胞质外蛋白的大量上调导致细胞包膜的重塑。正如其他 LiaSR TCS 所示，LiaSR(Lm) 被细胞壁活性抗生素激活。我们证明，诱导 LiaSR(Lm) 调节子所需的磷酸化 LiaR(Lm) 水平是由双功能传感器蛋白 LiaS(Lm) 的组氨酸激酶和磷酸酶活性之间的相互作用控制的。我们的数据表明，在没有细胞包膜应激的情况下，LiaS(Lm) 的磷酸酶活性受到 LiaF(Lm) 的刺激。
Most members of the phylum Firmicutes harbour a two-component system (TCS), LiaSR, which is involved in the response to cell envelope stress elicited most notably by inhibitors of the lipid II cycle. In all LiaSR systems studied in detail, LiaSR-mediated signal transduction has been shown to be negatively controlled by a membrane protein, LiaF, encoded upstream of liaSR. In this study we have analysed the LiaSR orthologue of Listeria monocytogenes (LiaSR(Lm)). Whole-genome transcriptional profiling indicated that activation of LiaSR(Lm) results in a remodelling of the cell envelope via the massive upregulation of membrane-associated and extracytoplasmic proteins in the presence of inducing stimuli. As shown for other LiaSR TCSs, LiaSR(Lm) is activated by cell wall-active antibiotics. We demonstrate that the level of phosphorylated LiaR(Lm), which is required for the induction of the LiaSR(Lm) regulon, is controlled by the interplay between the histidine kinase and phosphatase activities of the bifunctional sensor protein LiaS(Lm). Our data suggest that the phosphatase activity of LiaS(Lm) is stimulated by LiaF(Lm) in the absence of cell envelope stress.