Decreasing the Mitochondrial Synthesis of Malate in Potato Tubers Does Not Affect Plastidial Starch Synthesis, Suggesting That the Physiological Regulation of ADPglucose Pyrophosphorylase Is Context Dependent1[W][OA]
Modulation of the malate content of tomato ( Solanum lycopersicum ) fruit by altering the expression of mitochondrially localized enzymes of the tricarboxylic acid cycle resulted in enhanced transitory starch accumulation and subsequent effects on postharvest fruit physiology. In this study, we asse...
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Published in: | Plant physiology (Bethesda) Vol. 160; no. 4; pp. 2227 - 2238 |
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Main Authors: | , , , , , , |
Format: | Journal Article |
Language: | English |
Published: |
American Society of Plant Biologists
12-10-2012
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Subjects: | |
Online Access: | Get full text |
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Summary: | Modulation of the malate content of tomato (
Solanum lycopersicum
) fruit by altering the expression of mitochondrially localized enzymes of the tricarboxylic acid cycle resulted in enhanced transitory starch accumulation and subsequent effects on postharvest fruit physiology. In this study, we assessed whether such a manipulation would similarly affect starch biosynthesis in an organ that displays a linear, as opposed to a transient, kinetic of starch accumulation. For this purpose, we used RNA interference to down-regulate the expression of fumarase in potato (
Solanum tuberosum
) under the control of the tuber-specific B33 promoter. Despite displaying similar reductions in both fumarase activity and malate content as observed in tomato fruit expressing the same construct, the resultant transformants were neither characterized by an increased flux to, or accumulation of, starch, nor by alteration in yield parameters. Since the effect in tomato was mechanistically linked to derepression of the reaction catalyzed by ADP-glucose pyrophosphorylase, we evaluated whether the lack of effect on starch biosynthesis was due to differences in enzymatic properties of the enzyme from potato and tomato or rather due to differential subcellular compartmentation of reductant in the different organs. The results are discussed in the context both of current models of metabolic compartmentation and engineering. |
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Bibliography: | The author responsible for distribution of materials integral to the findings presented in this article in accordance with the policy described in the Instructions for Authors (www.plantphysiol.org) is: Alisdair R. Fernie (fernie@mpimp-golm.mpg.de). This work was supported by the Max Planck Society (to M.S., T.O., W.L.A., A.N.-N., and A.R.F.) and the European Union Collaborative Project 3-4. www.plantphysiol.org/cgi/doi/10.1104/pp.112.204826 The online version of this article contains Web-only data. Open Access articles can be viewed online without a subscription. |
ISSN: | 0032-0889 1532-2548 |
DOI: | 10.1104/pp.112.204826 |