The in vivo assembly and function of the N‐ and C‐terminal halves of the Tn 10‐encoded TetA protein in Escherichia coli

FEBS Letters

Someya, Yuichi¹  Yamaguchi, Akihito¹  Sawai, Tetsuo¹ 

[1] Division of Microhial Chemistry, Faculty of Pharmaceutical Sciences, Chiba University, 1-33 Yayoi-cho, Inage-ku, Chiba 263, Japan

关键词: Tetracycline;    Antiporter;    Gene separation;    Tetracycline/H+ antiporter;    In vivo assembly;   

DOI  :  10.1016/0014-5793(93)81378-D

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The tetA gene was cut into its N- and C-terminal halves at the central EcoRI site and the two halves were subcloned individually or together under a separate lac promoter/operator. The expression of the C-terminal half was detected with a C-terminal-specific antibody. The amount of the N-terminal half in the cytoplasmic membrane was not affected by the presence of the C-terminal half. In contrast, the amount of the C-terminal half in the membrane was increased in the presence of the N-terminal half, indicating that the N-terminal half helps the stable folding of the C-terminal half in the membrane. Each half individually showed no tetracycline transport activity, however, when both halves were expressed together, the resultant complex showed about 40% of the tetracycline transport activity of the wild-type per number of the C-terminals of TetA protein in the membrane.

【 授权许可】

Unknown