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Tree Physiology, 25:495–504
© 2005 Heron Publishing—Victoria, Canada
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Leaf responses of micropropagated apple plants to water stress: nonstructural carbohydrate composition and regulatory role of metabolic enzymes

Tian H. Li (1, 2) and Shao H. Li (1, 3)

1. Institute of Botany, The Chinese Academy of Sciences, 100093 Beijing, P.R. China / 2. Department of Fruit Science, College of Agronomy and Biotechnology, China Agricultural University, 100094 Beijing, P.R. China / 3. Corresponding author (shhli@ibcas.ac.cn) / Received June 25, 2004; accepted October 15, 2004; published online February 1, 2005

Summary

We examined changes in nonstructural carbohydrate biosynthesis and activities of related enzymes in leaves of micropropagated apple plants (Malus domestica Borkh. cv. ‘NaganoFuji’) in response to water stress, with particular emphasis on the enzymes associated with sorbitol, sucrose and starch metabolism. Water stress resulted in the accumulation of photosynthates in leaves, mainly sorbitol, sucrose, glucose and fructose, accompanied by a reduction in starch concentration. Correlation and path analysis indicated that water stress affected the partitioning of newly fixed carbon among terminal products. In response to water stress, ADP-glucose-pyrophosphorylase (ADPGPPase) activity decreased, becoming a critical and limiting step in shifting partitioning of photosynthetically fixed carbon. Amylase and ADPGPPase affected sucrose and sorbitol metabolism, mainly by regulating substrate supply; however, competition for limited substrate had a greater effect on the biosynthesis of sorbitol than of sucrose. Starch metabolism was also strictly regulated by ADPGPPase and amylase, whereas other related enzymes were downstream of the pathway for synthesis and degradation of carbohydrates and thus had relatively little effect on starch metabolism. Sorbitol dehydrogenase and sucrose phosphate synthase were critical regulators of sorbitol and sucrose metabolism, respectively.

Keywords: carbohydrate metabolism, carbon partitioning, enzyme activity, path analysis.


ISSN 0829-318X Copyright © 2002–2008 Heron Publishing