Role of Escherichia coli heat shock proteins IbpA and IbpB in protection of alcohol dehydrogenase AdhE against heat inactivation in the presence of oxygen

• Authors: Ewelina Matuszewska , Joanna Kwiatkowska , Elżbieta Ratajczak , Dorota Kuczyńska-Wiśnik , Ewa Laskowska
• Languages of publication: EN

Abstracts

EN

Escherichia coli small heat shock proteins IbpA and IbpB are molecular chaperones that bind denatured proteins and facilitate their subsequent refolding by the ATP-dependent chaperones DnaK/DnaJ/GrpE and ClpB. In vivo, the lack of IbpA and IbpB proteins results in increased protein aggregation under severe heat stress or delayed removal of aggregated proteins at recovery temperatures. In this report we followed the appearance and removal of aggregated alcohol dehydrogenase, AdhE, in E. coli submitted to heat stress in the presence of oxygen. During prolonged incubation of cells at 50°C, when AdhE was progressively inactivated, we initially observed aggregation of AdhE and thereafter removal of aggregated AdhE. In contrast to previous studies, the lack of IbpA and IbpB did not influence the formation and removal of AdhE aggregates. However, in ΔibpAB cells AdhE was inactivated and oxidized faster than in wild type strain. Our results demonstrate that IbpA and IbpB protected AdhE against thermal and oxidative inactivation, providing that the enzyme remained soluble. IbpA and IbpB were dispensable for the processing of irreversibly damaged and aggregated AdhE.

Keywords

EN

AdhE; protein aggregation; protein oxidation; small heat shock proteins IbpA and IbpB

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2009
• Volume: 56
• Issue: 1
• Pages: 55-61

Dates

published

2009

received

2008-08-04

revised

2009-01-12

accepted

2009-02-17

(unknown)

2009-02-24

Contributors

author

Ewelina Matuszewska

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

author

Joanna Kwiatkowska

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

author

Elżbieta Ratajczak

• Department of Cellular and Molecular Biology, Faculty of Biotechnology, University of Gdańsk, Gdańsk, Poland

author

Dorota Kuczyńska-Wiśnik

author

Ewa Laskowska

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

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