Rehosting of bacterial chaperones for high-quality protein production
| Autor: | Ugutz Unzueta, Rob Noad, Verónica Toledo-Rubio, Polly Roy, Mónica Martínez-Alonso, Antonio Villaverde, Neus Ferrer-Miralles |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2009 |
| Předmět: |
Protein Folding
endocrine system Gene Expression Heterologous Spodoptera medicine.disease_cause Applied Microbiology and Biotechnology law.invention law Gene expression Escherichia coli medicine Protein biosynthesis Animals HSP70 Heat-Shock Proteins Ecology biology Escherichia coli Proteins HSP40 Heat-Shock Proteins biology.organism_classification Recombinant Proteins Biochemistry Chaperone (protein) biology.protein Recombinant DNA bacteria Protein folding Bacteria Food Science Biotechnology |
| Zdroj: | Applied and environmental microbiology. 75(24) |
| ISSN: | 1098-5336 0099-2240 |
| Popis: | Coproduction of DnaK/DnaJ in Escherichia coli enhances solubility but promotes proteolytic degradation of their substrates, minimizing the yield of unstable polypeptides. Higher eukaryotes have orthologs of DnaK/DnaJ but lack the linked bacterial proteolytic system. By coexpression of DnaK and DnaJ in insect cells with inherently misfolding-prone recombinant proteins, we demonstrate simultaneous improvement of soluble protein yield and quality and proteolytic stability. Thus, undesired side effects of bacterial folding modulators can be avoided by appropriate rehosting in heterologous cell expression systems. |
| Databáze: | OpenAIRE |
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