纯度 | >90%SDS-PAGE. |
种属 | E.coli |
靶点 | mazE |
Uniprot No | P0AE72 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 1-82aa |
氨基酸序列 | MIHSSVKRWGNSPAVRIPATLMQALNLNIDDEVKIDLVDGKLIIEPVRKEPVFTLAELVNDITPENLHENIDWGEPKDKEVW |
预测分子量 | 16.8 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇关于mazE重组蛋白的参考文献及其摘要概括:
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1. **标题**:*"MazE-MazF interaction: A key regulator of bacterial programmed cell death"*
**作者**:Amitai S, Kolodkin-Gal I, Hananya-Meltabashi M, et al.
**摘要**:研究通过重组表达和纯化MazE蛋白,揭示其与毒素MazF的结合机制,证明MazE通过形成复合物抑制MazF的RNase活性,调控细菌应激反应中的程序性死亡。
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2. **标题**:*"Structural insights into the MazE-MazF toxin-antitoxin system by X-ray crystallography"*
**作者**:Christensen-Dalsgaard M, Gerdes K.
**摘要**:利用重组MazE和MazF蛋白进行共结晶,解析了复合物的三维结构,阐明MazE通过特定结构域结合MazF并阻断其毒性功能的分子基础。
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3. **标题**:*"Recombinant MazE as a potential inhibitor for controlling toxin activity in biotechnology applications"*
**作者**:Zhang Y, Inouye M, Li H.
**摘要**:报道重组MazE蛋白在大肠杆菌中的高效表达与纯化,验证其在体外抑制MazF切割RNA的能力,提出其在合成生物学中作为调控工具的潜力。
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注:以上文献信息为示例,实际引用时需核实具体期刊、年份及作者名称。建议通过PubMed或Web of Science以关键词“recombinant MazE”、“toxin-antitoxin MazEF”检索最新研究。
The mazEF toxin-antitoxin (TA) system, initially identified in *Escherichia coli*, is a genetic module comprising two components: MazF, a stable toxin, and MazE, a labile antitoxin. Under normal conditions, MazE binds to MazF, neutralizing its toxic activity. However, during stress conditions (e.g., nutrient deprivation, antibiotic exposure, or DNA damage), MazE is degraded by proteases, freeing MazF to inhibit cell growth or induce programmed cell death. This system is hypothesized to function as a stress-response mechanism, regulating bacterial population dynamics by eliminating damaged cells or promoting dormancy for survival.
Recombinant MazE protein, produced via genetic engineering in heterologous expression systems (e.g., *E. coli*), enables detailed study of its structure, function, and interaction with MazF. Structural analyses reveal MazE's intrinsically disordered N-terminal region, critical for binding MazF, and a structured C-terminal domain involved in conditional proteolysis. Researchers leverage recombinant MazE to investigate TA system regulation, particularly in bacterial persistence and antibiotic tolerance.
Beyond basic research, MazE has biotechnological and therapeutic potential. Engineered TA systems incorporating recombinant MazE are explored as synthetic biology tools for controlling gene expression or cell viability in industrial fermentation. In medicine, disrupting TA systems by targeting MazE-MazF interactions could sensitize bacteria to antibiotics, offering novel antimicrobial strategies. However, challenges remain, including understanding context-dependent TA system activation and optimizing recombinant MazE stability for applications.
Overall, the mazEF system exemplifies how bacterial stress adaptation mechanisms can be repurposed for scientific and practical goals, with recombinant MazE serving as a key tool in unraveling its complexity.
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