The Streptomyces rubiginosus xylose isomerase is missfolded when expressed in Saccharomyces cerevisiae.
(2003) In Enzyme and Microbial Technology 32(2). p.252-259- Abstract
- The Streptomyces rubiginosus xylA gene was cloned and expressed in Saccharomyces cerevisiae. No xylose isomerase activity could be detected. The produced xylose isomerase protein was insoluble and could only be recovered from cell lysates by extraction with the detergent sodium dodecyl-sulfate. In contrast, expression of the xylA gene from Thermus thermophilus in the same host strain resulted in soluble xylose isomerase protein with activities of 1 U mg−1 protein. Comparison of available 3D models suggests that the higher number of intra-subunit ion-bridges in the Thermus thermophilus xylose isomerase may stabilise the protein structure and promote folding by Saccharomyces cerevisiae.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/132789
- author
- Gárdonyi, Márk LU and Hahn-Hägerdal, Bärbel LU
- organization
- publishing date
- 2003
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Xylose isomerase, Saccharomyces cerevisiae, Protein folding, Xylose fermentation
- in
- Enzyme and Microbial Technology
- volume
- 32
- issue
- 2
- pages
- 252 - 259
- publisher
- Elsevier
- external identifiers
-
- wos:000180692300007
- scopus:0037415332
- ISSN
- 0141-0229
- DOI
- 10.1016/S0141-0229(02)00285-5
- language
- English
- LU publication?
- yes
- id
- c06ab3e9-ecbb-4d4d-99e9-cff1001718fb (old id 132789)
- date added to LUP
- 2016-04-01 12:10:33
- date last changed
- 2022-03-28 21:18:29
@article{c06ab3e9-ecbb-4d4d-99e9-cff1001718fb, abstract = {{The Streptomyces rubiginosus xylA gene was cloned and expressed in Saccharomyces cerevisiae. No xylose isomerase activity could be detected. The produced xylose isomerase protein was insoluble and could only be recovered from cell lysates by extraction with the detergent sodium dodecyl-sulfate. In contrast, expression of the xylA gene from Thermus thermophilus in the same host strain resulted in soluble xylose isomerase protein with activities of 1 U mg−1 protein. Comparison of available 3D models suggests that the higher number of intra-subunit ion-bridges in the Thermus thermophilus xylose isomerase may stabilise the protein structure and promote folding by Saccharomyces cerevisiae.}}, author = {{Gárdonyi, Márk and Hahn-Hägerdal, Bärbel}}, issn = {{0141-0229}}, keywords = {{Xylose isomerase; Saccharomyces cerevisiae; Protein folding; Xylose fermentation}}, language = {{eng}}, number = {{2}}, pages = {{252--259}}, publisher = {{Elsevier}}, series = {{Enzyme and Microbial Technology}}, title = {{The Streptomyces rubiginosus xylose isomerase is missfolded when expressed in Saccharomyces cerevisiae.}}, url = {{http://dx.doi.org/10.1016/S0141-0229(02)00285-5}}, doi = {{10.1016/S0141-0229(02)00285-5}}, volume = {{32}}, year = {{2003}}, }