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Optimizing cadmium and mercury specificity of CadR-based E. coli biosensors by redesign of CadR

Authors
  • Tao, Hu-Chun1
  • Peng, Zhi-Wen1
  • Li, Peng-Song1
  • Yu, Tai-An1
  • Su, Jie1
  • 1 School of Environment and Energy, Peking University Shenzhen Graduate School, Key Laboratory for Heavy Metal Pollution Control and Reutilization, Shenzhen, 518055, China , Shenzhen (China)
Type
Published Article
Journal
Biotechnology Letters
Publisher
Springer-Verlag
Publication Date
Apr 23, 2013
Volume
35
Issue
8
Pages
1253–1258
Identifiers
DOI: 10.1007/s10529-013-1216-4
Source
Springer Nature
Keywords
License
Yellow

Abstract

The metalloprotein, CadR, was redesigned to optimize cadmium and mercury specificity of CadR-based E. coli biosensors. By truncating 10 and 21 amino acids from the C-terminal extension of CadR, CadR-TC10 and CadR-TC21 were obtained, respectively. The genes cadR, cadR-TC10 and cadR-TC21 were used as sensing elements to construct green fluorescent protein based E.coli biosensors. Induction at 30 °C for 4 h in supplemented M9 medium was the optimized condition for the biosensor. Compared with CadR-based biosensor, there was a clear decline in induction coefficient for CadR-TC21-based biosensor (decreased by 86 % in Zn(II), 44 % in Hg(II), and only 37 % in Cd(II)). While in CadR-TC10-based biosensor, the induction coefficient decreased by 95 % in Zn(II), 70 % in Hg(II), and 67 % in Cd(II). Improved performances of CadR mutants based E. coli biosensors indicated that truncating C-terminal extension of CadR could improve the specificity.

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