A moonlighting role for LysM peptidoglycan binding domains underpins Enterococcus faecalis daughter cell separation.
A moonlighting role for LysM peptidoglycan binding domains underpins Enterococcus faecalis daughter cell separation.
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DOI：
10.1038/s42003-023-04808-z
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发表时间：
2023-04-18
影响因子：
5.9
通讯作者：
Mesnage, Stephane
中科院分区：
文献类型：
--
作者：
Salamaga, Bartlomiej;Turner, Robert D.;Elsarmane, Fathe;Galley, Nicola F.;Kulakauskas, Saulius;Mesnage, Stephane
控制细胞大小和形态对细菌适应性至关重要。在机会致病菌粪肠球菌中，双球菌和短细胞链的形成促进宿主的先天免疫逃避和传播。细胞链大小的最小化依赖于称为CRAMA的肽聚糖水解酶的活性，其专用于隔膜切割。为了防止自溶，在时间和空间上都严格控制CRAMA活性。在这里，我们表明，在隔膜的限制性本地化的RETAA发生通过一个意想不到的机制。我们证明，C-末端LysM结构域，允许酶结合肽聚糖是必不可少的，以针对这种酶的细胞内的隔膜，然后才易位跨膜。我们确定了一个膜结合的细胞质蛋白伴侣（称为AdmA）参与招聘的ESTRA通过其LysM域。这项工作揭示了兼职的作用LysM域，和机制的发展，以限制潜在的致命自溶素的亚细胞定位到其网站的行动。粪肠球菌肽聚糖水解酶A的C-末端LysM结构域对于这种自溶素在隔膜处的定位是必不可少的，其涉及膜结合的细胞质蛋白伴侣AdmA。
Control of cell size and morphology is of paramount importance for bacterial fitness. In the opportunistic pathogen Enterococcus faecalis, the formation of diplococci and short cell chains facilitates innate immune evasion and dissemination in the host. Minimisation of cell chain size relies on the activity of a peptidoglycan hydrolase called AtlA, dedicated to septum cleavage. To prevent autolysis, AtlA activity is tightly controlled, both temporally and spatially. Here, we show that the restricted localization of AtlA at the septum occurs via an unexpected mechanism. We demonstrate that the C-terminal LysM domain that allows the enzyme to bind peptidoglycan is essential to target this enzyme to the septum inside the cell before its translocation across the membrane. We identify a membrane-bound cytoplasmic protein partner (called AdmA) involved in the recruitment of AtlA via its LysM domains. This work reveals a moonlighting role for LysM domains, and a mechanism evolved to restrict the subcellular localization of a potentially lethal autolysin to its site of action. The C-terminal LysM domain of the Enterococcus faecalis peptidoglycan hydrolase AtlA is essential for the localization of this autolysin at the septum, which involves a membrane-bound cytoplasmic protein partner AdmA.
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影响因子：
2.8
作者：
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通讯作者：
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影响因子：
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