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. 1991 Jul;96(3):902–909. doi: 10.1104/pp.96.3.902

Sucrose-Induced Accumulation of β-Amylase Occurs Concomitant with the Accumulation of Starch and Sporamin in Leaf-Petiole Cuttings of Sweet Potato 1

Kenzo Nakamura 1, Masa-aki Ohto 1, Nobumasa Yoshida 1,2, Kyoko Nakamura 1
PMCID: PMC1080863  PMID: 16668273

Abstract

β-Amylase of sweet potato (Ipomoea batatas L.), which constitutes about 5% of the total soluble protein of the tuberous root, is absent or is present in only small amounts in organs other than the tuberous roots of the normal, field-grown plants. However, when leaf-petiole cuttings from such plants were supplied with a solution that contained sucrose, the accumulation of β-amylase was induced in both leaf and petiole portions of the explants. The sucrose-induced accumulation of β-amylase in leaf-petiole cuttings occurred concomitant with the accumulation of starch and of sporamin, the most abundant storage protein of the tuberous root. The accumulation of β-amylase, of sporamin and of starch in the petioles showed similar dependence on the concentration of sucrose, and a 6% solution of sucrose gave the highest levels of induction when assayed after 7 days of treatment. The induction of mRNAs for β-amylase and sporamin in the petiole could be detected after 6 hours of treatment with sucrose, and the accumulation of β-amylase and sporamin polypeptides, as well as that of starch, continued for a further 3 weeks. In addition to sucrose, glucose or fructose, but not mannitol or sorbitol, also induced the accumulation of β-amylase and sporamin, suggesting that metabolic effects of sucrose are important in the mechanism of this induction. Treatment of leaf-petiole cuttings with water under continuous light, but not in darkness, also caused the accumulation of small amounts of these components in the petioles, probably as a result of the endogenous supply of sucrose by photosynthesis. These results suggest that the expression of the gene for β-amylase is under metabolic control which is coupled with the expression of sink function of cells in the sweet potato.

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Selected References

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

  1. Bhatt R. M., Sharma R. C., Kohli V. K. Interspecific associations among anophelines in different breeding habitats of Kheda district, Gujarat. Part I: Canal irrigated area. Indian J Malariol. 1990 Sep;27(3):167–172. [PubMed] [Google Scholar]
  2. Caspar T., Lin T. P., Monroe J., Bernhard W., Spilatro S., Preiss J., Somerville C. Altered regulation of beta-amylase activity in mutants of Arabidopsis with lesions in starch metabolism. Proc Natl Acad Sci U S A. 1989 Aug;86(15):5830–5833. doi: 10.1073/pnas.86.15.5830. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Hattori T., Nakagawa S., Nakamura K. High-level expression of tuberous root storage protein genes of sweet potato in stems of plantlets grown in vitro on sucrose medium. Plant Mol Biol. 1990 Apr;14(4):595–604. doi: 10.1007/BF00027505. [DOI] [PubMed] [Google Scholar]
  4. Jefferson R., Goldsbrough A., Bevan M. Transcriptional regulation of a patatin-1 gene in potato. Plant Mol Biol. 1990 Jun;14(6):995–1006. doi: 10.1007/BF00019396. [DOI] [PubMed] [Google Scholar]
  5. Kreis M., Williamson M., Buxton B., Pywell J., Hejgaard J., Svendsen I. Primary structure and differential expression of beta-amylase in normal and mutant barleys. Eur J Biochem. 1987 Dec 15;169(3):517–525. doi: 10.1111/j.1432-1033.1987.tb13640.x. [DOI] [PubMed] [Google Scholar]
  6. LOWRY O. H., ROSEBROUGH N. J., FARR A. L., RANDALL R. J. Protein measurement with the Folin phenol reagent. J Biol Chem. 1951 Nov;193(1):265–275. [PubMed] [Google Scholar]
  7. Levi C., Preiss J. Amylopectin degradation in pea chloroplast extracts. Plant Physiol. 1978 Feb;61(2):218–220. doi: 10.1104/pp.61.2.218. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Lin T. P., Spilatro S. R., Preiss J. Subcellular localization and characterization of amylases in Arabidopsis leaf. Plant Physiol. 1988 Jan;86(1):251–259. doi: 10.1104/pp.86.1.251. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Lizotte P. A., Henson C. A., Duke S. H. Purification and Characterization of Pea Epicotyl beta-Amylase. Plant Physiol. 1990 Mar;92(3):615–621. doi: 10.1104/pp.92.3.615. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Mikami B., Morita Y., Fukazawa C. [Primary structure and function of beta-amylase]. Seikagaku. 1988 Mar;60(3):211–216. [PubMed] [Google Scholar]
  11. Ohta S., Hattori T., Morikami A., Nakamura K. High-level expression of a sweet potato sporamin gene promoter: beta-glucuronidase (GUS) fusion gene in the stems of transgenic tobacco plants is conferred by multiple cell type-specific regulatory elements. Mol Gen Genet. 1991 Mar;225(3):369–378. doi: 10.1007/BF00261676. [DOI] [PubMed] [Google Scholar]
  12. Paiva E., Lister R. M., Park W. D. Induction and accumulation of major tuber proteins of potato in stems and petioles. Plant Physiol. 1983 Jan;71(1):161–168. doi: 10.1104/pp.71.1.161. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Pan S. M., Chang T. C., Juang R. H., Su J. C. Starch Phosphorylase Inhibitor Is beta-Amylase. Plant Physiol. 1988 Dec;88(4):1154–1156. doi: 10.1104/pp.88.4.1154. [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Pongratz P., Beck E. Diurnal oscillation of amylolytic activity in spinach chloroplasts. Plant Physiol. 1978 Nov;62(5):687–689. doi: 10.1104/pp.62.5.687. [DOI] [PMC free article] [PubMed] [Google Scholar]
  15. Rocha-Sosa M., Sonnewald U., Frommer W., Stratmann M., Schell J., Willmitzer L. Both developmental and metabolic signals activate the promoter of a class I patatin gene. EMBO J. 1989 Jan;8(1):23–29. doi: 10.1002/j.1460-2075.1989.tb03344.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  16. Saeed M., Duke S. H. Amylases in Pea Tissues with Reduced Chloroplast Density and/or Function. Plant Physiol. 1990 Dec;94(4):1813–1819. doi: 10.1104/pp.94.4.1813. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Ziegler P., Beck E. Exoamylase activity in vacuoles isolated from pea and wheat leaf protoplasts. Plant Physiol. 1986 Dec;82(4):1119–1121. doi: 10.1104/pp.82.4.1119. [DOI] [PMC free article] [PubMed] [Google Scholar]

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