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

• Authors: Dorota Kuczyńska-Wiśnik , Dorota Żurawa-Janicka , Joanna Narkiewicz , Joanna Kwiatkowska , Barbara Lipińska , Ewa Laskowska
• Languages of publication: EN

Abstracts

EN

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.

Keywords

EN

protein aggregation; inclusion bodies; IbpA/B

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2004
• Volume: 51
• Issue: 4
• Pages: 925-931

Dates

published

2004

received

2004-07-09

revised

2004-10-15

accepted

2004-10-24

Contributors

author

Dorota Kuczyńska-Wiśnik

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

author

Dorota Żurawa-Janicka

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

author

Joanna Narkiewicz

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

author

Joanna Kwiatkowska

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

author

Barbara Lipińska

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

author

Ewa Laskowska

• Department of Biochemistry, University of Gdańsk, Gdańsk, Poland

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