Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Improved Coexpression and Multiassembly Properties of Recombinant Human Ferritin Subunits in Escherichia coli

  • Lee, Jung-Lim (Department of Food Science, Massachusetts Agricultural Experiment Station, University of Massachusetts) ;
  • Levin, Robert E. (Department of Food Science, Massachusetts Agricultural Experiment Station, University of Massachusetts) ;
  • Kim, Hae-Yeong (Institute of Life Sciences and Resources, and Graduate School of Biotechnology, Kyung Hee University)
  • Published : 2008.05.31
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Abstract

Human heavy chain (H-) and light chain (L-) ferritins were amplified from a human cDNA library. Each ferritin gene was inserted downstream of the T7 promoter of bacterial expression vectors, and two types of coexpression vectors were constructed. The expression levels of recombinant ferritins ranged about 26-36% of whole-cell protein. H-ferritin exhibited a lower expression ratio compared with L-ferritin, by a coexpression system. However, the coexpression of HL-ferritins was significantly increased above the expression ratio of H-ferritin by cultivation without IPTG induction overnight. Purified recombinant H-, L-, HL-, and LH-ferritins were shown to be homo- and heteropolymeric high molecular complexes and it was indicated that their assembled subunits would be able to work functionally in the cell. Thus, these results indicate an improvement in the expression strategy of H-ferritin for heteropolymeric production and studies of ferritin assembly in Escherichia coli.

Keywords

References

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