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Malate metabolism and reactions of oxidoreduction in cold-hardened winter rye (Secale cereale L.) leaves

Author:
Crecelius, F., Streb, P., Feierabend, J.
Source:
Journal of experimental botany 2003 v.54 no.384 pp. 1075-1083
ISSN:
0022-0957
Subject:
Secale cereale, leaves, malic acid, metabolism, enzyme activity, malate dehydrogenase, phosphoenolpyruvate carboxylase, malic enzyme, biochemical pathways
Abstract:
In cold-hardened leaves (CHL) of winter rye (Secale cereale L.) much higher levels of malate were detected by 13C-NMR than in non-hardened leaves (NHL). As this was not observed previously, malate metabolism of CHL was studied in more detail by biochemical assays. The activities of several enzymes of malate metabolism, NADP-malate dehydrogenase, NAD-malate dehydrogenase, phosphoenolpyruvate carboxylase, and NADP-malic enzyme, were also increased in CHL. Short exposures to low temperature of 1-3 d did not induce increases in the malate content or in the activities of enzymes of malate metabolism in mature NHL. The malate content and the enzyme activities declined within 1-2 d after a transfer of CHL from their growing temperature of 4 degrees C to 22 degrees C. The malate content was further increased when CHL were exposed to a higher light intensity at 4 degrees C. In CO2-free air the malate content of CHL strongly declined at 4 degrees C. Malate may thus serve as an additional carbon sink and as a CO2-store in CHL. It may further function as a vacuolar osmolyte balancing increased concentrations of soluble sugars previously observed in the cytosol of CHL. Malate was not used as a source of reductants when CHL were exposed to photo-oxidative stress by treatment with paraquat. However, the activities of enzymes of the oxidative pentose phosphate pathway were markedly increased in CHL and may serve as non-photosynthetic sources of NADPH and thus contribute to the previously observed superior capacity of CHL of winter rye to maintain their antioxidants in a reduced state in the presence of paraquat.
Agid:
1393866