Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD.

@article{Han2007SolubilizationOA,
  title={Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD.},
  author={K Han and J B Song and Keum-Young Ahn and Jin-Seung Park and Hyuk-Seong Seo and Jeewon Lee},
  journal={Protein engineering, design & selection : PEDS},
  year={2007},
  volume={20 11},
  pages={543-9}
}
The proteome profile of Escherichia coli BL21(DE3) generated in response to heat shock stress was analyzed by two-dimensional electrophoresis (2-DE), wherein we identified a FKBP-type peptidyl-prolyl cis-trans isomerse (PPIases), SlyD, as a stress-responsive (i.e. aggregation-resistant) protein. Even under an imposed severe stress condition where 29 out of 858 soluble proteins were totally eliminated and the synthesis levels of 171 proteins decreased over 5-fold, a 3.37-fold increase induced by… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 13 extracted citations

Similar Papers

Loading similar papers…