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

Journal of Proteome Research
Yew-Foon TanNicolas L Taylor

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 o...Continue Reading

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Citations

Sep 15, 2012·Planta·Chris CarrieJames Whelan
Dec 20, 2013·Plant Physiology·Fernanda SalvatoIan Max Møller
Feb 28, 2013·Plant & Cell Physiology·Keisuke YoshidaToru Hisabori
Mar 19, 2014·Frontiers in Plant Science·Hanna Janska, Malgorzata Kwasniak
Sep 10, 2016·Journal of Cell Science·Chris CarrieJürgen Soll
Mar 27, 2018·Physiologia Plantarum·Wei-Qing WangSong-Quan Song
Dec 14, 2019·Plant Methods·Yahui LiuLanping Guo
Jun 14, 2020·Mitochondrion·Marco ZancaniGiovanna Lippe

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