The N-domain of Escherichia coli phosphoglycerate kinase is a novel fusion partner to express aggregation-prone heterologous proteins

Jong Am Song, Dae Sung Lee, Jin Seung Park, Kyung Yeon Han, Jeewon Lee

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

As a fusion partner to express aggregation-prone heterologous proteins, we investigated the efficacy of Escherichia coli phosphoglycerate kinase (ePGK) that consists of two functional domains (N- and C-domain) and reportedly has a high structural stability. When the full-length ePGK (F-ePGK) was used as a fusion partner, the solubility of the heterologous proteins increased, but some of them still had a large fraction of insoluble aggregates. Surprisingly, the fusion expression using the N-domain of ePGK (N-ePGK) made the insoluble fraction significantly reduce to less than 10% for all the heterologous fusion proteins tested. Also, we evaluated the efficacy of N-ePGK in making the target proteins be expressed with their own native function or structure. It was found that of human ferritin light chain, bacterial arginine deiminase, human granulocyte colony stimulating factor were synthesized evidently with the self-assembly function, L-arginine-degrading activity, and the correct secondary structure, respectively, through the fusion expression using N-ePGK. These results indicate that N-ePGK is a highly potent fusion partner that can be widely used for the synthesis of a variety of heterologous proteins in E. coli.

Original languageEnglish
Pages (from-to)325-335
Number of pages11
JournalBiotechnology and Bioengineering
Volume109
Issue number2
DOIs
Publication statusPublished - 2012 Feb

Keywords

  • Aggregation-prone heterologous proteins
  • E. coli
  • Fusion partner
  • N-domain of PGK
  • Phosphoglycerate kinase (PGK)

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology

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