Streptococcus mutans cell division protein FtsZ has higher GTPase and polymerization activities in acidic environment
Streptococcus mutans cell division protein FtsZ has higher GTPase and polymerization activities in acidic environment
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DOI：
10.1111/omi.12364
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发表时间：
2022-03-13
影响因子：
3.7
通讯作者：
Wang, Xiaoyan
中科院分区：
文献类型：
--
作者：
Chen, Yuxing;Li, Yongliang;Wang, Xiaoyan
变形链球菌的耐酸性在其致龋过程中起重要作用。变形链球菌启动了一个强大的转录和生理适应机制，最终保护细胞机制免受酸损伤，并有助于细菌在酸性胁迫条件下的生存。虽然S.变形链球菌含有复杂的调控系统，已有研究表明变形链球菌是一种重要的致病菌。与大肠杆菌不同，变形杆菌不能维持中性的细胞内环境。当细胞外环境的pH降低时，细胞内pH平行降低。关于S.变异，特别是当涉及到关键的细胞骨架分裂蛋白FtsZ。在这项研究中，数据显示S.在酸性和中性环境中，变形菌的细胞分裂进程相似。在酸性环境中，分裂部位位于细胞中部，细胞质分裂均匀。此外，S.细胞中部的变形杆菌FtsZ不受酸性环境的影响。变形链球菌FtsZ在pH6.0的缓冲液中比在中性环境中具有更高的GTdR活性。此外，S.在酸性环境中对变形杆菌FtsZ的抑制作用强于中性环境。在S.变异株中，FtsZ氨基酸发生突变（E88K，L269K），S.变形杆菌FtsZ在酸性环境中显著降低。总的来说，S。在pH6.0的缓冲液中，变形杆菌FtsZ具有较高的体外功能活性。S.变形杆菌FtsZ受其特定氨基酸的影响。
The acid tolerance of Streptococcus mutans plays an important role in its cariogenic process. Streptococcus mutans initiates a powerful transcriptional and physiological adaptation mechanism, eventually shielding the cellular machinery from acid damage and contributing to bacterial survival under acidic stress conditions. Although S. mutans contains complex regulatory systems, existing studies have shown that S. mutans, unlike Escherichia coli, cannot maintain a neutral intracellular environment. As the pH of the extracellular environment decreases, the intracellular pH decreases in parallel. There is insufficient knowledge regarding the acid resistance of the intracellular proteins of S. mutans, particularly when it comes to the key cytoskeletal division protein FtsZ. In this study, the data showed that S. mutans had similar cell division progress in acidic and neutral environments. The splitting position was in the middle of cells, and the cytoplasm was divided evenly in the acidic environment. Additionally, the tread milling velocity of S. mutans FtsZ in the middle of cells was not affected by the acidic environment. Streptococcus mutans FtsZ had higher GTPase activity in pH 6.0 buffer than in the neutral environment. Furthermore, the polymerization of S. mutans FtsZ in the acidic environment was more robust than that in the neutral environment. After two particular amino acids of S. mutans, FtsZ amino acids were mutated (E88K, L269K), the polymerization of S. mutans FtsZ in the acidic environment was significantly reduced. Overall, S. mutans FtsZ exhibited higher functional activity in pH 6.0 buffer in vitro. The acid resistance of S. mutans FtsZ is affected by its particular amino acids.