GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae

Peng Fei Xia, Guo Chang Zhang, Jing Jing Liu, Suryang Kwak, Ching Sung Tsai, In Iok Kong, Bong Hyun Sung, Jung Hoon Sohn, Shu Guang Wang, Yong Su Jin

Research output: Contribution to journalArticlepeer-review


Rapid advances in the capabilities of reading and writing DNA along with increasing understanding of microbial metabolism at the systems-level have paved an incredible path for metabolic engineering. Despite these advances, post-translational tools facilitating functional expression of heterologous enzymes in model hosts have not been developed well. Some bacterial enzymes, such as Escherichia coli xylose isomerase (XI) and arabinose isomerase (AI) which are essential for utilizing cellulosic sugars, cannot be functionally expressed in Saccharomyces cerevisiae. We hypothesized and demonstrated that the mismatching of the HSP60 chaperone systems between bacterial and eukaryotic cells might be the reason these bacterial enzymes cannot be functionally expressed in yeast. The results showed that the co-expression of E. coli GroE can facilitate the functional expression of E. coli XI and AI, as well as the Agrobacterium tumefaciens D-psicose epimerase in S. cerevisiae. The co-expression of bacterial chaperonins in S. cerevisiae is a promising post-translational strategy for the functional expression of bacterial enzymes in yeast. Biotechnol. Bioeng. 2016;113: 2149–2155.

Original languageEnglish (US)
Pages (from-to)2149-2155
Number of pages7
JournalBiotechnology and bioengineering
Issue number10
StatePublished - Oct 1 2016


  • Escherichia coli
  • GroE chaperonins
  • Saccharomyces cerevisiae
  • metabolic engineering
  • post-translation
  • xylose isomerase

ASJC Scopus subject areas

  • Biotechnology
  • Bioengineering
  • Applied Microbiology and Biotechnology


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