Abstract:Abstract: Filamentous temperature-sensitive protein Z (FtsZ), a tubulin-like bacterial cell division protein, has been recognized as a potential new target and novel antibiotics target protein. In order to establish a high-purity separation and purification system of recombinant FtsZ and explore its enzymatic properties, the Mycobacterium tuberculosis FtsZ was expressed in Escherichia coli (E. coli) BL21 and purified by Ni-affinity chromatography and G-50 chromatography. The enzyme activity was determined by malachite green method and protein aggregation was determined by light scattering assays. The results showed that the Mycobacterium tuberculosis recombinant FtsZ with biological activities was obtained. Its relative molecular mass was about 49 kD, and the optimum temperature and pH were 37 ℃ and 6.8, respectively. In addition, the enzyme activity of FtsZ was promoted by Mg2+ and K+ and the GTP activity was strongly inhibited by DMSO or Triton X-100 if their volume fraction were higher than 0.1% and 0.005%, respectively (P<0.05). Furthermore, the polymerization of Mycobacterium tuberculosis FtsZ was quickly induced by the addition of GTP. The experiments provide a good foundation for further study and application of the Mycobacterium tuberculosis FtsZ.
引用本文:
代斌玲, 王爱莲, 高承贤, 闵真真, 钱朝东, 田应蓉, 陈建真. 结核分枝杆菌FtsZ的异源表达及酶学性质研究[J]. 生命科学研究, 2016, 20(6): 486-491.
DAI Bin-Ling, WANG Ai-Lian, GAO Cheng-Xian, MIN Zhen-Zhen, QIAN Chao-Dong, TIAN Ying-Rong, CHEN Jian-Zhen. Heterologous Expression and Characterization of FtsZ from Mycobacterium Tuberculosis. Life Science Research, 2016, 20(6): 486-491.