The impact of oxidative stress on Arabidopsis mitochondria.
- L. Sweetlove, J. Heazlewood, A. Millar
- BiologyThe Plant Journal
- 1 December 2002
Using H2O2 as a model stress, further work revealed that this treatment induced a protease activity in isolated mitochondria, putatively responsible for the degradation of oxidatively damaged mitochondrial proteins and that O2 consumption by mitochondria was significantly decreased by H2 O2 treatment.
Organization and regulation of mitochondrial respiration in plants.
- A. Millar, J. Whelan, K. Soole, D. Day
- Environmental Science, BiologyAnnual Review of Plant Biology
- 28 April 2011
Recent advances in understanding of the mitochondrial respiratory machinery of cells are described, including the presence of a classical oxidative phosphorylation system linked to the cytosol by transporters discussed alongside nonphosphorylating bypasses that alter the efficiency of ATP synthesis and play a role in oxidative stress responses in plants.
Salicylic Acid Is an Uncoupler and Inhibitor of Mitochondrial Electron Transport1
- C. Norman, K. A. Howell, A. Millar, J. Whelan, D. Day
- BiologyPlant Physiology
- 1 January 2004
SA is both an uncoupler and an inhibitor of mitochondrial electron transport and this underlies the induction of some genes by SA, and the possible implications for the interpretation of SA action in plants are discussed.
Oxygen affinity terminal oxidases in soybean mitochondria
- A. Millar, F. Bergersen, D. Day
- Biology
- 1 December 1994
The results indicate that the alternative oxidase cannot operate under the microaerobic conditions thought to prevail in nitrogen-fixing root nodules.
Experimental Analysis of the Arabidopsis Mitochondrial Proteome Highlights Signaling and Regulatory Components, Provides Assessment of Targeting Prediction Programs, and Indicates Plant-Specific…
- J. Heazlewood, Julian Tonti-Filippini, A. Gout, D. Day, J. Whelan, A. Millar
- BiologyThe Plant Cell Online
- 1 January 2004
Maps of putative orthology networks between yeast, human, and Arabidopsis mitochondrial proteomes and the Rickettsia prowazekii proteome provide detailed insights into the divergence of the plant mitochondrial proteome from those of other eukaryotes.
Molecular Distinction between Alternative Oxidase from Monocots and Dicots1
- M. Considine, R. Holtzapffel, D. Day, J. Whelan, A. Millar
- BiologyPlant Physiology
- 1 July 2002
The alternative oxidase (Aox) is encoded in two discrete gene subfamilies in higher plants. Aox1 is most widely known for its induction by stress stimuli in many tissues and is present in both…
Stress-induced co-expression of alternative respiratory chain components in Arabidopsis thaliana
- R. Clifton, R. Lister, J. Whelan
- Biology, Environmental SciencePlant Molecular Biology
- 23 May 2005
A series of treatment sets were identified, representing the response of specific AOX and NDH genes to mitochondrial inhibition, plastid inhibition and abiotic stresses, which emphasise the multiplicity of pathways affecting alternative electron transport components in plants.
METABOLITE TRANSPORT ACROSS SYMBIOTIC MEMBRANES OF LEGUME NODULES.
- M. Udvardi, D. Day
- Biology, Environmental ScienceAnnual Review of Plant Physiology and Plant…
- 1 June 1997
Infection of legume roots or stems with soil bacteria of the Rhizobiaceae results in the formation of nodules that become symbiotic nitrogen-fixing organs, and these form the focus of this review.
Post-transcriptional gene regulatory mechanisms in eukaryotes: an overview.
In this short review, selected examples of post-transcriptional gene regulatory mechanisms operating in both lower and higher eukaryotes will be used to highlight the plethora of such mechanisms already identified.
Lipoic Acid-Dependent Oxidative Catabolism of α-Keto Acids in Mitochondria Provides Evidence for Branched-Chain Amino Acid Catabolism in Arabidopsis1
- N. Taylor, J. Heazlewood, D. Day, A. Millar
- BiologyPlant Physiology
- 1 February 2004
Sequencing of peptides derived from trypsination of Arabidopsis mitochondrial proteins revealed the presence of many of the enzymes required for the oxidation of all three branched-chain amino acids.
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