PMID:15625564
| Citation |
Kuczyńska-Wiśnik, D, Zurawa-Janicka, D, Narkiewicz, J, Kwiatkowska, J, Lipińska, B and Laskowska, E (2004) Escherichia coli small heat shock proteins IbpA/B enhance activity of enzymes sequestered in inclusion bodies. Acta Biochim. Pol. 51:925-31 |
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| Abstract |
Escherichia coli small heat shock proteins, IbpA/B, function as molecular chaperones and protect misfolded proteins against irreversible aggregation. IbpA/B are induced during overproduction of recombinant proteins and bind to inclusion bodies in E. coli cells. We investigated the effect of DeltaibpA/B mutation on formation of inclusion bodies and biological activity of enzymes sequestered in the aggregates in E. coli cells. Using three different recombinant proteins: Cro-beta-galactosidase, beta-lactamase and rat rHtrA1 we demonstrated that deletion of the ibpA/B operon did not affect the level of produced inclusion bodies. However, in aggregates containing IbpA/B a higher enzymatic activity was detected than in the IbpA/B-deficient inclusion bodies. These results confirm that IbpA/B protect misfolded proteins from inactivation in vivo. |
| Links | |
| Keywords |
Animals; Escherichia coli/enzymology; Escherichia coli Proteins/genetics; Escherichia coli Proteins/physiology; Heat-Shock Proteins/genetics; Heat-Shock Proteins/physiology; Inclusion Bodies/enzymology; Inclusion Bodies/metabolism; Mutation; Rats; Recombinant Proteins/genetics; Recombinant Proteins/metabolism |
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