Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex.

Roberta Leonardi, Shirley A Fairhurst, Marco Kriek, David J Lowe, Peter L Roach

Department of Chemistry, University of Southampton, Highfield, Southampton SO17 1BJ, UK.

FEBS letters 2003 Mar 27

filter terms:

In Escherichia coli, two of the proteins required for the biosynthesis of the thiazole moiety of thiamine (vitamin B(1)) are ThiG and ThiH, encoded as part of the thiCEFSGH operon. In this study, a C-terminally hexahistidine-tagged ThiH (ThiH-His) was expressed in E. coli as a soluble protein from thiGH-His-tag and thiFSGH-His-tag-bearing plasmids. When isolated under anaerobic conditions, ThiG and ThiH-His co-purify as a large multimeric non-covalent complex. Electron paramagnetic resonance and UV-visible spectroscopy together with iron and sulfide analyses revealed the presence of an iron-sulfur cluster within this complex.

Citation

Roberta Leonardi, Shirley A Fairhurst, Marco Kriek, David J Lowe, Peter L Roach. Thiamine biosynthesis in Escherichia coli: isolation and initial characterisation of the ThiGH complex. FEBS letters. 2003 Mar 27;539(1-3):95-9