GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae. Issue 10 (6th April 2016)
- Record Type:
- Journal Article
- Title:
- GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae. Issue 10 (6th April 2016)
- Main Title:
- GroE chaperonins assisted functional expression of bacterial enzymes in Saccharomyces cerevisiae
- Authors:
- Xia, Peng‐Fei
Zhang, Guo‐Chang
Liu, Jing‐Jing
Kwak, Suryang
Tsai, Ching‐Sung
Kong, In Iok
Sung, Bong Hyun
Sohn, Jung‐Hoon
Wang, Shu‐Guang
Jin, Yong‐Su - Abstract:
- ABSTRACT: 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. © 2016 Wiley Periodicals, Inc. Abstract : This study demonstrated that the mismatching of HSP60 chaperonins between bacteria and yeast is the reason that some bacterial enzymes cannot be functionally expressed in Saccharomyces cerevisiae . A post‐translational tool is further developed to facilitatingABSTRACT: 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. © 2016 Wiley Periodicals, Inc. Abstract : This study demonstrated that the mismatching of HSP60 chaperonins between bacteria and yeast is the reason that some bacterial enzymes cannot be functionally expressed in Saccharomyces cerevisiae . A post‐translational tool is further developed to facilitating the functional expression of bacterial enzymes in S. cerevisiae via co‐expression of bacterial groE chaperonins. … (more)
- Is Part Of:
- Biotechnology and bioengineering. Volume 113:Issue 10(2016)
- Journal:
- Biotechnology and bioengineering
- Issue:
- Volume 113:Issue 10(2016)
- Issue Display:
- Volume 113, Issue 10 (2016)
- Year:
- 2016
- Volume:
- 113
- Issue:
- 10
- Issue Sort Value:
- 2016-0113-0010-0000
- Page Start:
- 2149
- Page End:
- 2155
- Publication Date:
- 2016-04-06
- Subjects:
- metabolic engineering -- Saccharomyces cerevisiae -- Escherichia coli -- GroE chaperonins -- post‐translation -- xylose isomerase
Biotechnology -- Periodicals
Bioengineering -- Periodicals
660.6 - Journal URLs:
- http://onlinelibrary.wiley.com/doi/10.1002/bip.v101.5/issuetoc ↗
http://www.interscience.wiley.com ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1002/bit.25980 ↗
- Languages:
- English
- ISSNs:
- 0006-3592
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 2089.850000
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 68.xml