Human G-CSF synthesis using stress-responsive bacterial proteins

Jong Am Song, Kyung Yeon Han, Jin Seung Park, Hyuk Seong Seo, Keum Young Ahn, Jeewon Lee

Research output: Contribution to journalArticlepeer-review

9 Citations (Scopus)


We previously reported that under the stress condition caused by the addition of 2-hydroxyethyl disulfide, a thiol-specific oxidant, to growing cultures of Escherichia coli BL21(DE3), a population of stress-responsive proteins [peptidyl-prolyl cis-trans isomerase B (PpiB), bacterioferritin (Bfr), putative HTH-type transcriptional regulator yjdC (YjdC), dihydrofolate reductase (FolA), chemotaxis protein cheZ (CheZ), and glutathione synthetase (GshB)] were significantly upregulated when compared with the nonstress condition. When those stress-responsive proteins were used as fusion partners for the expression of human granulocyte colony-stimulating factor (hG-CSF), the solubility of hG-CSF was dramatically enhanced in E. coli cytoplasm, whereas almost all of the directly expressed hG-CSF were aggregated to inclusion bodies. In addition, the spectra of circular dichroism measured with the purified hG-CSF were identical to that of standard hG-CSF, implying that the synthesized hG-CSF has native conformation. These results indicate that the bacterial stress-responsive proteins could be potent fusion expression partners for aggregation-prone heterologous proteins in E. coli cytoplasm.

Original languageEnglish
Pages (from-to)60-66
Number of pages7
JournalFEMS microbiology letters
Issue number1
Publication statusPublished - 2009 Jul


  • E. coli stress-responsive proteins
  • Escherichia coli BL21(DE3)
  • Fusion partner
  • G-CSF

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


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