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The Streptomyces rubiginosus xylose isomerase is missfolded when expressed in Saccharomyces cerevisiae.

Gárdonyi, Márk LU and Hahn-Hägerdal, Bärbel LU (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.
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author
organization
publishing date
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
language
English
LU publication?
yes
id
c06ab3e9-ecbb-4d4d-99e9-cff1001718fb (old id 132789)
date added to LUP
2007-06-28 11:54:36
date last changed
2018-05-29 09:20:46
@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},
  keyword      = {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/},
  volume       = {32},
  year         = {2003},
}