[Purification and DNA-binding of ToxR truncated protein of Vibrio parahaemolyticus].

  title={[Purification and DNA-binding of ToxR truncated protein of Vibrio parahaemolyticus].},
  author={Xiaoxu Hu and Yiquan Zhang and Qian Huang and Li Wang and Ruifu Yang and Xiaomin Li and Dongsheng Zhou and Qingping Zhong},
  journal={Wei sheng wu xue bao = Acta microbiologica Sinica},
  volume={54 8},
OBJECTIVE The DNA-binding domain of ToxR protein of Vibrio parahaemolyticus was expressed using the Escherichia coli BL21lambdaDE3 protein expression system, and its DNA-binding activity was characterized. METHODS The fragment of DNA-binding domain at N-terminal of ToxR (ToxR-N) was amplified by PCR from V. parahaemolyticus strain RIMD2210633, and then cloned into the BamHI and Hind III sites of the vector pET28a. The recombinant plasmid pET28a was transformed into BL21lambdaDE3. Over… CONTINUE READING