Biologia Plantarum

, Volume 44, Issue 3, pp 379–384

Mulberry Leaf Metabolism under High Temperature Stress


  • K.V. Chaitanya
    • School of Life SciencesPondicherry University
  • D. Sundar
    • School of Life SciencesPondicherry University
  • A. Ramachandra Reddy
    • School of Life SciencesPondicherry University

DOI: 10.1023/A:1012446811036

Cite this article as:
Chaitanya, K., Sundar, D. & Reddy, A.R. Biologia Plantarum (2001) 44: 379. doi:10.1023/A:1012446811036


Effects of high temperature on the activity of photosynthetic enzymes and leaf proteins were studied in mulberry (Morus alba L. cv. BC2-59). A series of experiments were conducted at regular intervals (120, 240 and 360 min) to characterize changes in activities of ribulose-1,5-bisphosphate carboxylase (RuBPC) and sucrose phosphate synthase (SPS), photosystem 2 (PS 2) activity, chlorophyll (Chl), carotenoid (Car), starch, sucrose (Suc), amino acid, free proline, protein and nucleic acid contents in leaves under high temperature (40 °C) treatments. High temperature markedly reduced the activities of RuBPC and SPS in leaf extracts. Chl content and PS 2 activity in isolated chloroplasts were also affected by high temperature, particularly over 360 min treatment. Increased leaf temperature affected sugar metabolism through reductions in leaf starch content and sucrose-starch balance. While total soluble protein content decreased under heat, total amino acid content increased. Proline accumulation (1.5-fold) was noticed in high temperature-stressed leaves. A reduction in the contents of foliar nitrogen and nucleic acids (DNA and RNA) was also noticed. SDS-PAGE protein profile showed few additional proteins (68 and 85 kDa) in mulberry plants under heat stress compared to control plants. Our results clearly suggest that mulberry plants are very sensitive to high temperature with particular reference to the photosynthetic carbon metabolism.

chlorophyllMorus albanucleic acidsphotosynthesisphotosystem 2proteinsRuBP carboxylasesucrose phosphate synthase
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© Kluwer Academic Publishers 2001