Characterization of disulfide exchange between DsbA and HtrA proteins from Escherichia coli

• Authors: Joanna Skórko-Glonek , Anna Sobiecka-Szkatuła , Barbara Lipińska
• Languages of publication: EN

Abstracts

EN

DsbA is the major oxidase responsible for generation of disulfide bonds in proteins of E. coli envelope. In the present work we provided the first detailed characterization of disulfide exchange between DsbA and its natural substrate, HtrA protease. We demonstrated that HtrA oxidation relies on DsbA, both in vivo and in vitro. We followed the disulfide exchange between these proteins spectrofluorimetrically and found that DsbA oxidizes HtrA with a 1 : 1 stoichiometry. The calculated second-order apparent rate constant (kapp) of this reaction was 3.3 × 104 ± 0.6 × 104 M-1s-1. This value was significantly higher than the values obtained for nonfunctional disulfide exchanges between DsbA and DsbC or DsbD and it was comparable to the kapp values calculated for in vitro oxidation of certain non-natural DsbA substrates of eukaryotic origin.

Keywords

EN

DsbA oxidoreductase; disulfide exchange; HtrA protease; stoichiometry of HtrA-DsbA interaction; kinetics of HtrA oxidation

• Publisher: Polish Biochemical Society
• Journal: Acta Biochimica Polonica
• Year: 2006
• Volume: 53
• Issue: 3
• Pages: 585-589

Dates

published

2006

received

2006-03-20

revised

2006-08-30

accepted

2006-09-16

(unknown)

2006-10-01

Contributors

author

Joanna Skórko-Glonek

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

author

Anna Sobiecka-Szkatuła

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

author

Barbara Lipińska

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

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