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

• Autorzy: Matuszewska E. , Kwiatkowska J. , Ratajczak E. , Kuczynska-Wisnik D. , Laskowska E.
• Języki publikacji: EN

Abstrakty

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 50oC, 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.

Słowa kluczowe

EN

heat stress; heat inactivation; IbpA protein; oxygen; AdhE aggregate; IbpB protein; alcohol dehydrogenase; protein aggregation; Escherichia coli; protein oxidation; heat shock protein

• Wydawca: -
• Czasopismo: Acta Biochimica Polonica
• Rocznik: 2009
• Tom: 56
• Numer: 1
• Opis fizyczny: p.55-61,fig.,ref.

Twórcy

autor

Matuszewska E.

• University of Gdansk, Kladki 24, 80-952 Gdansk, Poland

autor

Kwiatkowska J.

autor

Ratajczak E.

autor

Kuczynska-Wisnik D.

autor

Laskowska E.

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