Mercuric ion uptake by escherichia coli cells producing thiobacillus ferrooxidans merC

Chihiro Inoue, Tomonobu Kusano, Simon Silver

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


The merC gene of Thiobacillus ferrooxidans was overexpressed in Escherichia coli under the control of the tac promoter. MerC protein synthesized in E. coli has a N-terminal amino acid sequence of S-A-I-X-R-I-I-D-K-I-G-I-V-G-, which agrees with the amino acid sequence deduced from its nucleotide sequence except that an initiating methionine residue was removed. The MerC protein was localized in the particulate (membrane) cell fraction, and not in the soluble cytoplasmic fraction. E. coli cells carrying a plasmid containing the tac promoter-directed merC showed 203Hg2+ uptake in an isopropyl-1-thio-β-d-galactopyranoside (IPTG)-dependent manner.

Original languageEnglish
Pages (from-to)1289-1292
Number of pages4
JournalBioscience, Biotechnology and Biochemistry
Issue number8
Publication statusPublished - 1996 Jan
Externally publishedYes


  • Gene expression
  • Merc
  • Mercuric ion
  • Thiobacillus ferrooxidans
  • Transport

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry


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