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J. Biol. Chem., Vol. 282, Issue 52, 37436-37447, December 28, 2007

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The Cytotoxic Lipid Peroxidation Product 4-Hydroxy-2-nonenal Covalently Modifies a Selective Range of Proteins Linked to Respiratory Function in Plant Mitochondria^*

Alison M. Winger¹, Nicolas L. Taylor², Joshua L. Heazlewood², David A. Day, and A. Harvey Millar³

From the Australian Research Council Centre of Excellence in Plant Energy Biology, the University of Western Australia, 35 Stirling Highway, Crawley 6009, Western Australia and Australian Research Council Centre of Excellence in Plant Energy Biology, School of Biological Sciences, University of Sydney, 2006 New South Wales, Australia

Plants encounter a variety of environmental stresses that affect their cellular machinery and that they adapt to on a daily basis. Lipid peroxidation is one consequence, at the cellular level, of such stresses and yields cytotoxic lipid aldehydes, including 4-hydroxy-2-nonenal (HNE), that react with specific sites in proteins, leading to diverse changes in protein function and/or stability. We have assessed the sensitivity of plant mitochondrial proteins to HNE modification, using one-dimensional and two-dimensional denaturing PAGE and blue native-PAGE coupled to immunological detection and tandem mass spectrometry identification. A select range of proteins was modified by exogenous application of HNE to mitochondria isolated from Arabidopsis cell cultures. These included a number of proteins that directly interact with the ubiquinone pool, as well as a number of soluble matrix proteins. Mitochondria isolated from cell cultures following hydrogen peroxide, antimycin A, or menadione treatment had significantly reduced respiratory capacity and elevated levels of HNE adduction to specific subsets of proteins. Targets identified included the proteins affected by direct application of HNE but also some new proteins, including a number of matrix dehydrogenases, the inner membrane adenine nucleotide translocator, and the outer membrane voltage-dependent anion channel. Degradation products of some proteins were also found to be HNE adducted, suggesting a link between HNE adduction and protein turnover. Some of the major enzyme complexes that were HNE adducted did not show demonstrable changes in their maximal activity measured with artificial acceptors, but changes did occur in associations between respiratory chain complexes following stress treatments.

Received for publication, March 20, 2007 , and in revised form, October 17, 2007.

^* This work was supported in part by grants from the Australian Research Council through the Centres of Excellence Program (to A. H. M. and D. A. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Tables S1–S7.

¹ Recipient of an Australian postgraduate award.

² Supported as Australian Research Council postdoctoral fellow.

³ Supported as Australian Research Council professorial fellow. To whom correspondence should be addressed. Tel.: 61-8-6488-7245; Fax: 61-8-6488-4401; E-mail: hmillar{at}cyllene.uwa.edu.au.

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