Prx (peroxiredoxin) 2 protects cells from deleterious oxidative damage. It catalyses the breakdown of hydroperoxides through a highly reactive cysteine residue and has been linked to chaperone activity that promotes cell survival under conditions of oxidative stress. It may also be involved in redox signalling by binding to other proteins. In the present study we have searched for binding partners of Prx2 in H2O2-treated Jurkat and human umbilical vein endothelial cells and discovered that the hyperoxidized form selectively co-precipitated with the protein disulfide-isomerase ERp46. Mutant analyses revealed that loss of the peroxidative cysteine residue of Prx2 also facilitated complex formation with ERp46, even without H2O2 treatment, whereas the resolving cysteine residue of Prx2 was indispensible for the interaction to occur. The complex involved a stable non-covalent interaction that was disassociated by the reduction of intramolecular disulfides in ERp46, or by disruption of the decameric structure of hyperoxidized Prx2. This is the first example of a protein interaction dependent on the hyperoxidized status of a Prx.
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Research Article|
July 12 2013
Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide- isomerase ERp46
Paul E. Pace;
Paul E. Pace
1Centre for Free Radical Research, Department of Pathology, University of Otago, P.O. Box 4345, Christchurch 8140, New Zealand
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Alexander V. Peskin;
Alexander V. Peskin
1Centre for Free Radical Research, Department of Pathology, University of Otago, P.O. Box 4345, Christchurch 8140, New Zealand
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Min-Hi Han;
Min-Hi Han
1Centre for Free Radical Research, Department of Pathology, University of Otago, P.O. Box 4345, Christchurch 8140, New Zealand
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Mark B. Hampton;
Mark B. Hampton
1Centre for Free Radical Research, Department of Pathology, University of Otago, P.O. Box 4345, Christchurch 8140, New Zealand
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Christine C. Winterbourn
Christine C. Winterbourn
1
1Centre for Free Radical Research, Department of Pathology, University of Otago, P.O. Box 4345, Christchurch 8140, New Zealand
1To whom correspondence should be addressed (email christine.winterbourn@otago.ac.nz).
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Publisher: Portland Press Ltd
Received:
January 04 2013
Revision Received:
May 23 2013
Accepted:
May 28 2013
Accepted Manuscript online:
May 28 2013
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2013 Biochemical Society
2013
Biochem J (2013) 453 (3): 475–485.
Article history
Received:
January 04 2013
Revision Received:
May 23 2013
Accepted:
May 28 2013
Accepted Manuscript online:
May 28 2013
Citation
Paul E. Pace, Alexander V. Peskin, Min-Hi Han, Mark B. Hampton, Christine C. Winterbourn; Hyperoxidized peroxiredoxin 2 interacts with the protein disulfide- isomerase ERp46. Biochem J 1 August 2013; 453 (3): 475–485. doi: https://doi.org/10.1042/BJ20130030
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