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2004 | 51 | 4 | 925-931
Article title

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

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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 ΔibpA/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-β-galactosidase, β-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.
Physical description
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
  • Department of Biochemistry, University of Gdańsk, Gdańsk, Poland
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