pr3003535_si_003.pdf (456.53 kB)
Components of Mitochondrial Oxidative Phosphorylation Vary in Abundance Following Exposure to Cold and Chemical Stresses
journal contribution
posted on 2012-07-06, 00:00 authored by Yew-Foon Tan, A. Harvey Millar, Nicolas L. TaylorPlant 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.