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J Proteome Res. 2012 Jul 6;11(7):3860-79. doi: 10.1021/pr3003535. Epub 2012 May 31.

Components of mitochondrial oxidative phosphorylation vary in abundance following exposure to cold and chemical stresses.

Author information

1
ARC Centre of Excellence in Plant Energy Biology, MCS Building M316, The University of Western Australia, 35 Stirling Highway, Crawley WA 6009, Western Australia, Australia.

Abstract

Plant mitochondria are highly responsive organelles that vary their metabolism in response to a wide range of chemical and environmental conditions. Quantitative proteomics studies have begun to allow the analysis of these large-scale protein changes in mitochondria. However studies of the integral membrane proteome of plant mitochondria, arguably the site responsible for the most fundamental mitochondrial processes of oxidative phosphorylation, protein import and metabolite transport, remain a technical challenge. Here we have investigated the changes in protein abundance in response to a number of chemical stresses and cold. In addition to refining the subcellular localization of 66 proteins, we have been able to characterize 596 protein × treatment combinations following a range of stresses. To date it has been assumed that the main mitochondrial response to stress involved the induction of alternative respiratory proteins such as AOX, UCPs, and alternative NAD(P)H dehydrogenases; we now provide evidence for a number of very specific protein abundance changes that have not been highlighted previously by transcript studies. This includes both previously characterized stress responsive proteins as well as major components of oxidative phosphorylation, protein import/export, and metabolite transport.

PMID:
22574745
DOI:
10.1021/pr3003535
[Indexed for MEDLINE]

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