PMID:15168861
| Citation |
Petersson, L, Carrió, MM, Vera, A and Villaverde, A (2004) The impact of dnaKJ overexpression on recombinant protein solubility results from antagonistic effects on the control of protein quality. Biotechnol. Lett. 26:595-601 |
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| Abstract |
We have produced increasing levels of DnaK and its co-chaperone DnaJ along with the model VP1LAC misfolding-prone protein, to explore the role of DnaK on the management of Escherichia coli inclusion bodies. While relative solubility of VP1LAC is progressively enhanced, the heat-shock response is down-regulated as revealed by decreasing levels of GroEL. This is accompanied by an increasing yield of VP1LAC and a non-regular evolution of its insoluble fraction, at moderate levels of DnaK resulting in more abundant inclusion bodies. Also, the impact of chaperone co-expression is much more pronounced in wild type cells than in a DnaK- mutant, probably due to the different background of heat shock proteins in these cells. The involvement of DnaK in the supervision of misfolding proteins is then pictured as a dynamic balance between its immediate holding and folding activities, and the side-effect downregulation of the heat shock response though the limitation of other chaperone and proteases activities. |
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| Keywords |
Dimerization; Escherichia coli/enzymology; Escherichia coli/genetics; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; Gene Expression Regulation, Bacterial/physiology; Gene Expression Regulation, Enzymologic/physiology; HSP40 Heat-Shock Proteins; HSP70 Heat-Shock Proteins/chemistry; HSP70 Heat-Shock Proteins/genetics; HSP70 Heat-Shock Proteins/metabolism; Heat-Shock Proteins; Heat-Shock Response/physiology; Inclusion Bodies/chemistry; Inclusion Bodies/genetics; Inclusion Bodies/metabolism; Protein Binding; Protein Engineering/methods; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Solubility |
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