Abstract
The effect of light on NADPH-protochlorophyllide oxidoreductase and its mRNA has been studied in five different species of dicotyledonous plants, bean (Phaseolus vulgaris L.), pea (Pisum sativum L.), tomato (Lycopersicon esculentum Mill.), sunflower (Helianthus annuns L.) and mustard (Sinapis alba L.), and in two monocotyledonous plant species, maize (Zea mays L.) and barley (Hordeum vulgare L.). In all these species, illumination of etiolated seedlings led to a rapid decline of both the activity and the content of the enzyme protein. These results indicate that there may be a general light-dependent regulation of the enzyme common to higher plants.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Abbreviations
- Pchlide reductase:
-
NADPH-protochlorophyllide oxidoreductase
References
Apel, K., Santel, HJ., Redlinger, T.E., Falk, H. (1980) The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Isolation and characterisation of the NADPH-protochlorophyllide oxidoreductase. Eur. J. Biochem. 111, 251–258
Apel, K. (1981) The protochlorophyllide holochrome of barley (Hordeum vulgare L.). Phytochrome-induced decrease of translatable mRNA coding for the NADPH-protochlorophyllide oxidoreductase. Eur. J. Biochem. 120, 89–93
Aviv, H., Leder, P. (1972) Purification of biologically active globin messenger RNA by chromatography on thymidylic acid-cellulose. Proc. Natl. Acad. Sci. USA 69, 1408–1412
Batschauer, A., Apel, K. (1984) An inverse control by phytochrome of the expression of two nuclear genes in barley (Hordeum vulgare L.). Eur. J. Biochem. 143, 593–597
Batschauer, A., Mösinger, E., Kreuz, K., Dörr, I., Apel, K. (1986) The implication of a plastid-derived factor in the transcriptional control of nuclear genes encoding the light-harvesting chlorophyll a/b protein. Eur. J. Biochem. 154, 625–634
Chirgwin, J.M., Przybyla, A.E., McDonald, R.J., Rutter, W.J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in nucleases. Biochem. 18, 5294–5304
Dehesh, K., Klaas, M., Häuser, I., Apel, K. (1986a) Light-induced changes in the distribution of the 36000-Mr, polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.). I. Localisation by immunoblotting in isolated plastids and total leaf extracts. Planta 169, 162–171
Dehesh, K., v. Cleve, B., Ryberg, M., Apel, K. (1986b) Lightinduced changes in the distribution of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase within different cellular compartments of barley (Hordeum vulgare L.). II. Localisation by immunogold labelling in ultrathin sections of barley leaves. Planta 169, 172–183
Griffiths, W.T. (1974) Source of reducing equivalents for the invitro synthesis of chlorophyll from protochlorophyll. FEBS Lett. 46, 301–304
Griffiths, W.T.(1978) Reconstitution of chlorophyllide formation by isolated etioplast membranes.Biochem. J., 681–692
Häuser, I., Dehesh, K., Apel, K. (1984) The proteolytic degradation in-vitro of the NADPH-protochlorophyllide oxidoreductase of barley (Hordeum vulgare L.). Arch. Biochem. Biophys. 228, 577–586
Häuser, I., Dehesh, K., Apel, K. (1987) Light-induced changes in the amount of the 36000-Mr polypeptide of NADPH-protochlorophyllide oxidoreductase and its mRNA in barley plants grown under a diurnal light/dark cycle. Planta 170, 453–460
Harpster, M., Apel, K. (1985) The light-dependent regulation of gene expression during plastid development in higher plants. Physiol. Plant. 64, 147–152
Ikeuchi, M., Murakami, S. (1982) Behaviour of the 36000-Dalton protein in the internal membran of squash etioplasts during greening. Plant Cell Physiol. 23, 575–583
Kay, St. A., Griffiths, W.T. (1983) Light induced breakdown of NADPH-protochlorophyllide oxidoreductase in-vitro. Plant Physiol. 72, 229–236
Kay, St. A., Keith, B., Shinozaki, K., Chye, M.-L., Chua, N.-H. (1989) The rice phytochrome gene: structure, autoregulated expression, and binding of GT-1 to a conserved site in the 5′upstream region. Plant Cell 1, 351–360
Klein, R.R., Gamble, P.E., Mullet, J.E. (1988) Light dependent accumulation of radiolabeled plastid-encoded chlorophyll a-apoprotein requires chlorophyll a. II. Analysis of chlorophyll-deficient mutants and phytochrome involvement. Plant Physiol. 88, 1246–1256
Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature 227, 680–685
Laing, W., Kreuz, K., Apel, K. (1988) Light-dependent, but phytochrome-independent, translational control of the accumulation of the P700 chlorophyll-a protein of photosystem I in barley (Hordeum vulgare L.). Planta 176, 269–276
Lissemore, J.L., Colbert, J.T., Quail, P.H. (1987) Cloning of cDNA for phytochrome from etiolated cucurbita and coordinate photoregulation of the abundance of two distinct phytochrome transcripts. Plant Mol Biol. 8, 485–496
Lütz, C., Nordmann, U. (1983) The localization of saponins in prolamellar bodies mainly depends on the isolation of etioplasts. Z. Pflanzenphysiol. 110, 201–210
Mapleston, E.R., Griffiths, W.T. (1980) Light modulation of the activity of the protochlorophyllide oxidoreductase. Biochem. J. 189, 125–133
Meyer, G., Bliedung, H., Kloppstech, K. (1983) NADPH-protochlorophyllide oxidoreductase: Reciprocal regulation in mono- and dicotyledonean plants. Plant Cell Rep. 2, 26–29
Mösinger, E., Batschauer, A., Schäfer, E., Apel, K. (1985) Phytochrome control of in-vitro transcription of specific genes in isolated nuclei from barley (Hordeum vulgare L.). Eur. J. Biochem. 147, 136–142
Quail, P.H., Colbert, J.T., Peters, N.K., Christensen, A.H., Sharrock, R.A., Lissemore, J.L. (1986) Phytochrome and the regulation of the expression of its genes. Philos Trans. R. Soc. London, Ser. B 314, 469–480
Ryberg, M., Dehesh, K. (1986) Localisation of NADPH-protochlorophyllide oxidoreductase in dark grown wheat (Triticum aestivum) by immuno-electron microscopy before and after transformation of the prolamellar bodies. Physiol. Plant 66, 616–624
Santel, H.J., Apel, K. (1981) The protochlorophyllide holochrome of barley (Hordeum vulgare L.). The effect of light on the NADPH-protochlorophyllide oxidoreductase. Eur. J. Biochem. 120, 95–103
Shropshire, W. jr., Mohr, H., eds. (1983) Encyclopedia of plant physiology, N.S. vol. 16A: Photomorphogenesis. Springer, Berlin Heidelberg New York Tokyo
Schulz, R., Steinmüller, K., Klaas, M., Forreiter, C., Rasmussen, S., Hiller, C., Apel, K. (1989) Nucleotide sequence of a cDNA coding for the NADPH-protochlorophyllide oxidoreductase (PCR) of barley (Hordeum vulgare L.) and its expression in Escherichia coli. Mol. Gen. Genet. 217, 355–361
Towbin, M., Staehelin, T., Gordon, J. (1979) Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets; procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350–4354
Westhoff, P., Schrubar, H., Oswald, A., Streubel, M., Offermann, K. (1990) Biogenesis of photosystem II in C3 and C4 plants-a model system to study developmentally regulated and cellspecific expression of plastid genes. In: Current research in photosynthesis, vol. 3, pp. 483–490, Baltschewsky, M., ed. Kluwer, Dortrecht
Author information
Authors and Affiliations
Additional information
Didicated to Professor H. Mohr on the occasion of his 60th birthday
We are grateful to P. Westhoff and H. Schrubar (Botanisches Institut, Universität Düsseldorf, FRG) for making available to us their data on the Pchlide reductase of Sorghum bicolor prior to publication and for sending us seeds of this plant species. This work has been supported by the Deutsche Forschungsgemeinschaft.
Rights and permissions
About this article
Cite this article
Forreiter, C., van Cleve, B., Schmidt, A. et al. Evidence for a general light-dependent negative control of NADPH-protochlorophyllide oxidoreductase in angiosperms. Planta 183, 126–132 (1991). https://doi.org/10.1007/BF00197576
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00197576