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变形链球菌细胞分裂蛋白 FtsZ 在酸性环境中有更高的 GTPase 和聚合活性。

Streptococcus mutans cell division protein FtsZ has higher GTPase and polymerization activities in acidic environment.

机构信息

Department of Cardiology and Endodontology & National Clinical Research Center for Oral Disease, School and Hospital of Stomatology, Peking University, Beijing, P. R. China.

Department of Geriatric Dentistry, School and Hospital of Stomatology, Peking University, Beijing, P. R. China.

出版信息

Mol Oral Microbiol. 2022 Jun;37(3):97-108. doi: 10.1111/omi.12364. Epub 2022 Mar 13.

DOI:10.1111/omi.12364
PMID:35218317
Abstract

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.

摘要

变形链球菌的耐酸性在其致龋过程中起着重要作用。变形链球菌启动了强大的转录和生理适应机制,最终使细胞机制免受酸的损伤,并有助于细菌在酸性应激条件下存活。尽管变形链球菌含有复杂的调控系统,但现有研究表明,与大肠杆菌不同,变形链球菌不能维持中性的细胞内环境。随着细胞外环境 pH 值的降低,细胞内 pH 值也随之降低。目前对于变形链球菌细胞内蛋白的耐酸性知之甚少,特别是对于关键的细胞骨架分裂蛋白 FtsZ 更是如此。在这项研究中,数据表明变形链球菌在酸性和中性环境中具有相似的细胞分裂进程。分裂位置在细胞中部,细胞质在酸性环境中均匀分裂。此外,变形链球菌 FtsZ 在细胞中部的 tread milling 速度不受酸性环境的影响。变形链球菌 FtsZ 在 pH6.0 缓冲液中的 GTPase 活性高于中性环境。此外,变形链球菌 FtsZ 在酸性环境中的聚合比中性环境更稳定。在两个特定的变形链球菌 FtsZ 氨基酸(E88K,L269K)发生突变后,变形链球菌 FtsZ 在酸性环境中的聚合明显减少。总的来说,变形链球菌 FtsZ 在体外 pH6.0 缓冲液中表现出更高的功能活性。变形链球菌 FtsZ 的耐酸性受其特定氨基酸的影响。

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Streptococcus mutans cell division protein FtsZ has higher GTPase and polymerization activities in acidic environment.变形链球菌细胞分裂蛋白 FtsZ 在酸性环境中有更高的 GTPase 和聚合活性。
Mol Oral Microbiol. 2022 Jun;37(3):97-108. doi: 10.1111/omi.12364. Epub 2022 Mar 13.
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Glutamate 83 and arginine 85 of helix H3 bend are key residues for FtsZ polymerization, GTPase activity and cellular viability of Escherichia coli: lateral mutations affect FtsZ polymerization and E. coli viability.螺旋 H3 上的谷氨酸 83 和精氨酸 85 是 FtsZ 聚合、GTP 酶活性和大肠杆菌细胞活力的关键残基:侧链突变会影响 FtsZ 聚合和大肠杆菌的活力。
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Bacterial SOS checkpoint protein SulA inhibits polymerization of purified FtsZ cell division protein.细菌SOS检查点蛋白SulA抑制纯化的FtsZ细胞分裂蛋白的聚合。
J Bacteriol. 1998 Aug;180(15):3946-53. doi: 10.1128/JB.180.15.3946-3953.1998.
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FtsZ polymerization assays: simple protocols and considerations.FtsZ聚合分析:简单方案及注意事项。
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Glutamate-induced assembly of bacterial cell division protein FtsZ.谷氨酸诱导细菌细胞分裂蛋白FtsZ的组装。
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GTP-dependent polymerization of Escherichia coli FtsZ protein to form tubules.大肠杆菌FtsZ蛋白的GTP依赖性聚合形成微管。
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Cationic lipid enhances assembly of bacterial cell division protein FtsZ: a possible role of bacterial membrane in FtsZ assembly dynamics.阳离子脂质增强细菌细胞分裂蛋白 FtsZ 的组装:细菌膜在 FtsZ 组装动力学中的可能作用。
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The GTPase activity of Escherichia coli FtsZ determines the magnitude of the FtsZ polymer bundling by ZapA in vitro.大肠杆菌FtsZ的GTP酶活性在体外决定了ZapA对FtsZ聚合物的成束程度。
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Dr-FtsA, an actin homologue in Deinococcus radiodurans differentially affects Dr-FtsZ and Ec-FtsZ functions in vitro.Dr-FtsA是耐辐射球菌中的一种肌动蛋白同源物,在体外对Dr-FtsZ和Ec-FtsZ的功能有不同影响。
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Discovery of a small molecule that inhibits cell division by blocking FtsZ, a novel therapeutic target of antibiotics.发现一种通过阻断FtsZ(一种新型抗生素治疗靶点)来抑制细胞分裂的小分子。
J Biol Chem. 2003 Nov 7;278(45):44424-8. doi: 10.1074/jbc.M307625200. Epub 2003 Sep 2.

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