Glycolytic Enzymes Associate Dynamically with Mitochondria in Response to Respiratory Demand and Support Substrate Channeling (original) (raw)

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aDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom

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aDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom

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aDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom

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bMax-Planck Institute for Molecular Plant Physiology, 14476, Potsdam-Golm, Germany

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aDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom

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aDepartment of Plant Sciences, University of Oxford, Oxford, OX1 3RB, United Kingdom

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Revision received:

21 September 2007

Accepted:

15 October 2007

Published:

02 November 2007

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James W.A. Graham, Thomas C.R. Williams, Megan Morgan, Alisdair R. Fernie, R. George Ratcliffe, Lee J. Sweetlove, Glycolytic Enzymes Associate Dynamically with Mitochondria in Response to Respiratory Demand and Support Substrate Channeling, The Plant Cell, Volume 19, Issue 11, November 2007, Pages 3723–3738, https://doi.org/10.1105/tpc.107.053371
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Abstract

In Arabidopsis thaliana, enzymes of glycolysis are present on the surface of mitochondria and free in the cytosol. The functional significance of this dual localization has now been established by demonstrating that the extent of mitochondrial association is dependent on respiration rate in both Arabidopsis cells and potato (Solanum tuberosum) tubers. Thus, inhibition of respiration with KCN led to a proportional decrease in the degree of association, whereas stimulation of respiration by uncoupling, tissue ageing, or overexpression of invertase led to increased mitochondrial association. In all treatments, the total activity of the glycolytic enzymes in the cell was unaltered, indicating that the existing pools of each enzyme repartitioned between the cytosol and the mitochondria. Isotope dilution experiments on isolated mitochondria, using 13C nuclear magnetic resonance spectroscopy to monitor the impact of unlabeled glycolytic intermediates on the production of downstream intermediates derived from 13C-labeled precursors, provided direct evidence for the occurrence of variable levels of substrate channeling. Pull-down experiments suggest that interaction with the outer mitochondrial membrane protein, VDAC, anchors glycolytic enzymes to the mitochondrial surface. It appears that glycolytic enzymes associate dynamically with mitochondria to support respiration and that substrate channeling restricts the use of intermediates by competing metabolic pathways.

© 2007 American Society of Plant Biologists

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