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Intracellular redistribution of phytochrome in etiolated soybean (Glycine max L.) seedlings

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The intracellular distribution of phytochrome in hypocotyl hooks of etiolated soybean (Glycine max L.) has been examined by immunofluorescence using a newly produced monoclonal antibody (Soy-1) directed to phytochrome purified from etiolated soybean shoots. Cortical cells in the hook region exhibit the strongest phytochrome-associated fluorescence, which is diffusely distributed throughout the cytosol in unirradiated, etiolated seedlings. A redistribution of immunocytochemically detectable hytochrome to discrete areas (sequestering) following irradiation with red light requires a few minutes at room temperature in soybean, whereas this redistribution is reversed rapidly following irradiation with far-red light. In contrast, sequestering in oat (Avena sativa L.) occurs within a few seconds (D. McCurdy and L. Pratt, 1986, Planta 167, 330–336) while its reversal by far-red light requires hours (J. M. Mackenzie Jr. et al., 1975, Proc. Natl. Acad. Sci. USA 72, 799–803). The time courses, however, of red-light-enhanced phytochrome pelletability and sequestering are similar for soybean as they are for oat. Thus, while these observations made with a dicotyledon are consistent with the previous conclusion derived from work with oat, namely that sequestering and enhanced pelletability are different manifestations of the same intracellular event, they are inconsistent with the hypothesis that either is a primary step in the mode of action of phytochrome.

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differential interference contrast


far-red light



Pfr, P:

far-red- and red-absorbing form of phytochrome, respectively


red light


  1. Butler, W.L., Norris, K.H. (1960) The spectrophotometry of dense light-scattering material. Arch. Biochem. Biophys. 87, 31–40

  2. Coleman, R.A., Pratt, L.H. (1974a) Electron microscopic localization of phytochrome in plants using an indirect antibody-labeling method. J. Histochem. Cytochem. 22, 1039–1047

  3. Coleman, R.A., Pratt, L.H. (1974b) Subcellular localization of the red-absorbing form of phytochrome by immunocytochemistry. Planta 121, 119–131

  4. Cope, M. (1991) Comparative analysis of the intracellular redistribution of phytochrome in etiolated soybean seedlings. Doct. Dissert., University of Georgia, Athens, USA

  5. Cordonnier, M.-M., Smith, C., Greppin, H., Pratt, L.H. (1983) Production and purification of monoclonal antibodies to Pisum and Avena phytochrome. Planta 158, 369–376

  6. Cordonnier, M.-M., Greppin, H., Pratt, L.H. (1985) Monoclonal antibodies with differing affinities to the red-absorbing and far-red-absorbing forms of phytochrome. Biochemistry 24, 3246–3253

  7. Epel, B.L., Butler, W.L., Pratt, L.H. Tokuyasu, K.T. (1980) Immunofluorescence localization studies of the Pr and Pfr forms of phytochrome in the coleoptile tips of oats, corn and wheat. In: Photoreceptors and plant development. European Photomorphogenesis Symposium, Antwerp, 1979, pp. 121–133, De Greef J., ed. Antwerpen University Press, Antwerp

  8. Johnson, G.D., Nogueira Araujo, M. de C. (1981) A simple method of reducing the fading of immunofluorescence during microscopy. J. Immunol. Methods 43, 349–350

  9. Mackenzie, J.M. Jr., Coleman, R.A., Briggs, W.R., Pratt, L.H. (1975) Reversible redistribution of phytochrome within the cell upon conversion to its physiologically active form. Proc. Natl. Acad. Sci. USA 72, 799–803

  10. McCurdy, D.W., Pratt, L.H. (1986a) Immunogold electron microscopy of phytochrome in Avena: identification of intracellular sites responsible for phytochrome sequestering and enhanced pelletability. J. Cell Biol. 103, 2541–2550

  11. McCurdy, D.W., Pratt, L.H. (1986b) Kinetics of intracellular redistribution of phytochrome in Avena coleoptiles after its photoconversion to the active, far-red-absorbing form. Planta 167, 330–336

  12. Pratt, L.H. (1984) Phytochrome purification. In: Techniques in photomorphogenesis, pp. 175–200, Smith, H., Holmes, M.G., eds. Academic Press, London New York

  13. Pratt, L.H. (1986) Localization within the plant. In: Photomorphogenesis in plants, pp. 61–81, Kendrick, R.E., Kronenberg, G.H.M., eds. Martinus Nijhoff Publishers, Dordrecht

  14. Pratt, L.H., Marmé, D. (1976) Red light-enhanced phytochrome pelletability: re-examination and further characterization. Plant Physiol. 58, 686–692

  15. Pratt, L.H., Wampler, J.E., Rich, E.S. (1985) An automated dualwavelength spectrophotometer optimized for phytochrome assay. Anal. Instrum. 13, 269–287

  16. Pratt, L.H., McCurdy, D.W., Shimazaki, Y., Cordonnier, M.-M. (1986) Immunodetection of phytochrome: immunocytochemistry, immunoblotting, and immunoquantitation. Mod. Methods Plant Anal. New Ser. 4, 50–74

  17. Quail, P. H. (1983) Rapid action of phytochrome in photomorphogenesis. In: Encyclopedia of plant physiology, N.S., vol. 16A: Photomorphogenesis, pp. 178–212, Shropshire, W. Jr., Mohr, H., eds. Springer, Berlin Heidelberg New York Tokyo

  18. Quail, P.H., Briggs, W.R. (1978) Irradiation-enhanced phytochrome pelletability: requirement for phosphorylative energy in vivo. Plant Physiol. 62, 773–778

  19. Saunders, M.J., Cordonnier, M.-M., Palevitz, B.A., Pratt, L.H. (1983) Immunofluorescence visualization of phytochrome in Pisum sativum L. epicotyls using monoclonal antibodies. Planta 159, 545–553

  20. Shimazaki, Y., Pratt, L.H. (1985) Immunochemical detection with rabbit polyclonal and mouse monoclonal antibodies of different pools of phytochrome from etiolated and green Avena shoots. Planta 164, 333–344

  21. Speth, V., Otto, V., Schäfer, E. (1986) Intracellular localisation of phytochrome in oat coleoptiles by electron microscopy. Planta 168, 299–304

  22. Speth, V., Otto, V., Schäfer, E. (1987) Intracellular localisation of phytochrome and ubiquitin in red-light-irradiated oat coleoptiles by electron microscopy. Planta 171, 332–338

  23. Thompson, L.K., Pratt, L.H., Cordonnier, M.-M., Kadwell, S., Darlix, J.-L., Crossland, L. (1989) Fusion protein-based epitope mapping of phytochrome: precise identification of an evolutionarily conserved domain. J. Biol. Chem. 264, 12426–12431

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This work was supported by National Science Foundation grant No. DCB-8703057.

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Cope, M., Pratt, L.H. Intracellular redistribution of phytochrome in etiolated soybean (Glycine max L.) seedlings. Planta 188, 115–122 (1992). https://doi.org/10.1007/BF00198947

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Key words

  • Glycine (phytochrome)
  • Intracellular localization (phytochrome)
  • Monoclonal antibody (phytochrome)
  • Phytochrome (immunocytochemistry)