Article
Solubilization of aggregation-prone heterologous proteins by covalent fusion of stress-responsive Escherichia coli protein, SlyD.
Protein engineering, design & selection : PEDS - 1 Nov 2007
Han Kyung-Yeon, Song Jong-Am, Ahn Keum-Young, Park Jin-Seung, Seo Hyuk-Seong, Lee Jeewon
Abstract excerpt
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...
Topics
- Escherichia coli
- Escherichia coli Proteins
- Gene Expression
- Genetic Vectors
- Heat-Shock Response
- Hot Temperature
- Microbial Viability
- Mutation
- Peptidylprolyl Isomerase
- Protein Engineering
- Proteome
- Recombinant Fusion Proteins
- Solubility