Skip to main content
Plant Physiology logoLink to Plant Physiology
. 1988 Jul;87(3):727–730. doi: 10.1104/pp.87.3.727

Sink Metabolism in Tomato Fruit 1

I. Developmental Changes in Carbohydrate Metabolizing Enzymes

Nina L Robinson 1,2, John D Hewitt 1,3, Alan B Bennett 1
PMCID: PMC1054828  PMID: 16666215

Abstract

In developing tomato (Lycopersicon esculentum Mill.) fruit, starch levels reach a peak early in development with soluble sugars (hexoses) gradually increasing in concert with starch degradation. To determine the enzymic basis of this transient partitioning of carbon to starch, the activities of key carbohydrate-metabolizing enzymes were investigated in extracts from developing fruits of three varieties (cv VF145-7879, cv LA1563, and cv UC82B), differing in final soluble sugar accumulation. Of the enzymes analyzed, ADPglucose pyrophosphorylase and sucrose synthase levels were temporally correlated with the transient accumulation of starch, having highest activities in cv LA1563, the high soluble sugar accumulator. Of the starch-degrading enzymes, phosphorylase levels were fivefold higher than those of amylase, and these activities did not increase during the period of starch degradation. Fiften percent of the amylase activity and 45 to 60% of the phosphorylase activity was localized in the chloroplast in cv VF145-7879. These results suggest that starch degradation in tomato fruit is predominantly phosphorolytic. The results suggest that starch biosynthetic capacity, as determined by levels of ADPglucose pyrophosphorylase rather than starch degradative capacity, regulate the transient accumulation of starch that occurs early in tomato fruit development. The results also suggest that ADPglucose pyrophosphorylase and sucrose synthase levels correlated positively with soluble sugar accumulation in the three varieties examined.

Full text

PDF
727

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Arnon D. I. COPPER ENZYMES IN ISOLATED CHLOROPLASTS. POLYPHENOLOXIDASE IN BETA VULGARIS. Plant Physiol. 1949 Jan;24(1):1–15. doi: 10.1104/pp.24.1.1. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Damon S., Hewitt J., Nieder M., Bennett A. B. Sink Metabolism in Tomato Fruit : II. Phloem Unloading and Sugar Uptake. Plant Physiol. 1988 Jul;87(3):731–736. doi: 10.1104/pp.87.3.731. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Fish L. E., Jagendorf A. T. High rates of protein synthesis by isolated chloroplasts. Plant Physiol. 1982 Oct;70(4):1107–1114. doi: 10.1104/pp.70.4.1107. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. Okita T. W., Greenberg E., Kuhn D. N., Preiss J. Subcellular localization of the starch degradative and biosynthetic enzymes of spinach leaves. Plant Physiol. 1979 Aug;64(2):187–192. doi: 10.1104/pp.64.2.187. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. Salerno G. L., Gamundi S. S., Pontis H. G. A procedure for the assay of sucrose synthetase and sucrose phosphate synthetase in plant homogenates. Anal Biochem. 1979 Feb;93(1):196–199. [PubMed] [Google Scholar]
  6. Schaffner W., Weissmann C. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal Biochem. 1973 Dec;56(2):502–514. doi: 10.1016/0003-2697(73)90217-0. [DOI] [PubMed] [Google Scholar]
  7. Spilatro S. R., Preiss J. Regulation of Starch Synthesis in the Bundle Sheath and Mesophyll of Zea mays L. : Intercellular Compartmentalization of Enzymes of Starch Metabolism and the Properties of the ADPglucose Pyrophosphorylases. Plant Physiol. 1987 Mar;83(3):621–627. doi: 10.1104/pp.83.3.621. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Yelle S., Hewitt J. D., Robinson N. L., Damon S., Bennett A. B. Sink Metabolism in Tomato Fruit : III. Analysis of Carbohydrate Assimilation in a Wild Species. Plant Physiol. 1988 Jul;87(3):737–740. doi: 10.1104/pp.87.3.737. [DOI] [PMC free article] [PubMed] [Google Scholar]

Articles from Plant Physiology are provided here courtesy of Oxford University Press

RESOURCES