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Escherichia coli small heat shock proteins IbpA-B enhance activity of enzymes sequestered in inclusion bodies

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Kuczynska-Wisnik D., Zurawa-Janicka D., Narkiewicz J., Kwiatkowska J., Lipinska B., Laskowska E.

Acta Biochimica Polonica

2004

tom 51

nr 4

Escherichia coli small heat shock proteins, IbpA/B, function as molecular chape- rones 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 AibpA/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-ß-galactosidase, ß-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.

Ograniczanie wyników

1 Acta Biochimica Polonica

1 Kuczynska-Wisnik D.

1 Kwiatkowska J.

1 Laskowska E.

1 Lipinska B.

1 Narkiewicz J.

1 Zurawa-Janicka D.

1 2004

Wyniki wyszukiwania

Escherichia coli small heat shock proteins IbpA-B enhance activity of enzymes sequestered in inclusion bodies