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Molecular properties of phosphoenolpyruvate carboxylase from C3, C3−C4 intermediate, and C4 Flaveria species

  • Published: February 1986
  • Volume 167, pages 218–225 (1986)
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Molecular properties of phosphoenolpyruvate carboxylase from C3, C3−C4 intermediate, and C4 Flaveria species
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  • C. A. Adams1 nAff2,
  • F. Leung1 &
  • S. S. M. Sun1 
  • 106 Accesses

  • 20 Citations

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Abstract

Phosphoenolpyruvate carboxylase (PEPCase; EC 4.1.1.31) from Flaveria trinervia Mohr (C4), F. floridana Johnston (C3−C4), and F. cronquistii Powell (C3) leaves were compared by electrotransfer blotting/enzyme-linked immunoassay (Western-blot analysis), mobility of the native enzyme in polyacrylamide gels and in isoelectric focusing (IEF) gels, peptide mapping, and in-vitro translation of RNA isolated from each plant. The PEPCases from the C3 and C3−C4 plants were very similar to each other in terms of electrophoretic mobilities on gels and isoenzyme patterns on IEF gels, and identical in peptide mapping. Quantitative differences were noted, however, in that the C3−C4 intermediate plant contained more PEPCase overall and that the relative activity of individual isoenzymes shifted between the C3 and C3−C4 intermediate PEPCases. The PEPCase from the C4 plant had a different isoenzyme pattern, a different peptide map, and was far more abundant than the other two enzymes. Western blot analysis demonstrated the cross-reactivity of PEPCases from all three Flaveria species with antibody raised against maize PEPCase. The results provide evidence, at the molecular level, that supports the view of C3−C4 intermediate species as C3-like plants with some C4-like photosynthetic characteristics, but there are differences from the C3 plant in the quantity and properties of the PEPCase from the C3−C4 intermediate plant.

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Abbreviations

IEF:

isoelectric focusing

kDa:

kilodalton

PEPCase:

phosphoenolpyruvate carboxylase

Rubisco:

Ribulose-1,5-bisphosphate carboxylase/oxygenase

References

  • Apel, P., Maass, I. (1981) Photosynthesis in species of Flaveria. CO2 compensation concentration, O2 influence on photosynthetic gas exchange and δ13C values in species of Flaveria (Asteraceae). Biochem. Physiol. Pflanzen 176, 396–399

    Google Scholar 

  • Apel, P., Ohle, H. (1979) CO2-Kompensationspunkt und Blattanatomie bei Arten der Gattung Moricandia DC. (Cruciferae). Biochem. Physiol. Pflanz. 174, 68–75

    Google Scholar 

  • Arnon, D.I. (1949) Copper enzymes in isolated chloroplasts. Polyphenoloxidase in Beta vulgaris. Plant Physiol. 24, 1–15

    Google Scholar 

  • Bauwe, H. (1984) Photosynthetic enzyme activities and immunofluorescence studies on the localization of ribulose-1,5-bisphosphate carboxylase/oxygenase in leaves of C3, C4, and C3−C4 intermediate species of Flaveria (Asteraceae). Biochem. Physiol. Pflanz. 179, 253–268

    Google Scholar 

  • Bradford, M.M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248–254

    Google Scholar 

  • Brown, R.H., Brown, W.V. (1975) Photosynthetic characteristics of Panicum milioides, a species with reduced photorespiration. Crop Sci. 15, 681–685

    Google Scholar 

  • Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J., Rutter, W.J. (1979) Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochemistry 18, 5294–5299

    Google Scholar 

  • Cleveland, D.W., Fischer, S.G., Kirschner, M.W., Laemmli, U.K. (1977) Peptide mapping by limited proteolysis in sodium dodecyl sulfate and analysis by gel electrophoresis. J. Biol. Chem. 252, 1102–1106

    Google Scholar 

  • Edwards, G.E., Huber, S.C. (1981) The C4 pathway. In: The biochemistry of plants, vol. 8: Photosynthesis, pp. 237–281, Hatch, M.D., Boardman, N.K., eds. Academic Press, New York London Toronto Sydney

    Google Scholar 

  • Gerwick, B.C., Ku, S.B., Black, C.C. (1980) Initiation of sulfate activation: A variation in C4 photosynthesis plants. Science 209, 513–515

    Google Scholar 

  • Hall, T.C., Ma, Y., Buchbinder, B.U., Pyne, J.W., Sun, S.M., Bliss, F.A. (1978) Messenger RNA for G1 protein of French bean seeds: cell-free translation and product characterization. Proc. Natl. Acad. Sci. USA 75, 3196–3200

    Google Scholar 

  • Hatch, M.D., Slack, C.R. (1970) Photosynthetic CO2-fixation pathways. Annu. Rev. Plant Physiol. 21, 141–162

    Google Scholar 

  • Hatch, M.D., Osmond, C.B., Troughton, J.H., Björkman, O. (1971) Physiological and biochemical characteristics of C3 and C4 Atriplex species and hybrids in relation to the evolution of the C4 pathway. Carnegie Inst. Washington YrbK. 71, 135–141

    Google Scholar 

  • Hattersley, P.W., Watson, L., Osmond, C.B. (1977) In situ immuno fluorescent labeling of ribulose 1,5-bisphosphate carboxylase in leaves of C3 and C4 plants. Aust. J. Plant Physiol. 4, 523–539

    Google Scholar 

  • Holaday, A.S., Lee, K.W., Chollet, R. (1984) C3−C4 intermediate species in the genus Flaveria: leaf anatomy, ultrastructure, and the effect of O2 on the CO2 compensation concentration. Planta 160, 25–32

    Google Scholar 

  • Johnson, D.A., Gautsch, J.W., Sportsman, J.R., Elder, J.H. (1984) Improved technique utilizing nonfat dry milk for analysis of proteins and nucleic acids transferred to nitrocellulose. Gene Anal. Techn. 1, 3–8

    Google Scholar 

  • Kanai, R., Edwards, G.E. (1973) Separation of mesophyll protoplasts and bundle sheath cells from maize leaves for photosynthetic studies. Plant Physiol. 51, 1133–1137

    Google Scholar 

  • Kennedy, R.A., Laetsch, W.M. (1974) Plant species intermediate for C3, C4 photosynthesis. Science 184, 1087–1089

    Google Scholar 

  • Ku, M.S.B., Monson, R.K., Littlejohn, R.O.Jr., Nakamoto, H., Fisher, D.B., Edwards, G.E. (1983) Photosynthetic characteristics of C3−C4 intermediate Flaveria species I. Leaf anatomy, photosynthetic responses to O2 and CO2, and activities of key enzymes in the C3 and C4 pathways. Plant Physiol. 71, 944–948

    Google Scholar 

  • Laemmli, U.K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680–685

    Google Scholar 

  • Moore, R., Black, C.C.Jr. (1979) Nitrogen assimilation pathways in leaf mesophyll and bundle sheat cells of C4 photosynthesis plants formulated from comparative studies with Digitaria sanguinalis (L.) Scop. Plant Physiol. 64, 309–313

    Google Scholar 

  • Nakamoto, H., Ku, M.S.B., Edwards, G.E. (1983) Photosynthetic characteristics of C3−C4 intermediate Flaveria species. II. Kinetic properties of phosphoenolpyruvate carboxylase from C3, C4 and C3−C4 intermediate species. Plant Cell Physiol. 24, 1387–1393

    Google Scholar 

  • Palmiter, R.D. (1973) Ovalbumin messenger ribonucleic acid translation. Comparable rates of polypeptide initiation and elongation on ovalbumin and globin messenger ribonucleic acid in a rabbit reticulocyte lysate. J. Biol. Chem. 248, 2095–2106

    Google Scholar 

  • Powell, A.M. (1978) Systematics of Flaveria (Flaveriinae-Asteraceae). Ann. Missouri Bot Gard. 65, 590–636

    Google Scholar 

  • Ray, T.B., Black, C.C. (1979) The C4 pathway and its regulation. In: Encyclopedia of plant physiology, N.S., vol. 6: Photosynthesis II, pp. 77–101, Gibbs, M., Latzko, E., eds. Springer, Berlin Heidelberg New York

    Google Scholar 

  • Reed, J.E., Chollet, R. (1985) Immunofluorescent localization of phosphoenolpyruvate carboxylase and ribulose 1,5-bisphosphate carboxylase/oxygenase proteins in leaves of C3, C4 and C3−C4 intermediate Flaveria species. Planta 165, 439–445

    Google Scholar 

  • Riezman, H., Weir, E.M., Leaver, C.J., Titus, D.E., Becker, W.M. (1980) Regulation of glyoxysomal enzymes during germination of cucumber, 3. In vitro translation and characterization of four glyoxysomal enzymes. Plant Physiol. 65, 40–46

    Google Scholar 

  • Rumpho, M.E., Ku, M.S.B., Cheng, S.-H., Edwards, G.E. (1984) Photosynthetic characteristics of C3−C4 intermediate Flaveria species. III. Reduction of photorespiration by a limited C4 pathway of photosynthesis in Flaveria ramosissima. Plant Physiol. 75, 993–996

    Google Scholar 

  • Scrutton, M.C., Fatebene, F. (1975) An assay system for localisation of pyruvate and phosphoenolpyruvate carboxylase activity on polyacrylamide gels and its application to detection of these enzymes in tissue and cell extracts. Anal. Biochem. 69, 247–260

    Google Scholar 

  • Sims, T.L., Hague, D.R. (1981) Light-stimulated increase of translatable mRNA for phosphoenolpyruvate carboxylase in leaves of maize. J. Biol. Chem. 256, 8252–8255

    Google Scholar 

  • Smith, B.N., Powell, A.M. (1984) C-4-like F-1 hybrid: C-3XC-4 Flaveria species. Naturwissenschaften 71, 217–218

    Google Scholar 

  • Ting, I.P., Osmond, C.B. (1973) Photosynthetic phosphoenolpyruvate carboxylases. Characteristics of alloenzymes from leaves of C3 and C4 plants. Plant Physiol. 51, 439–447

    Google Scholar 

  • Uedan, K., Sugiyama, T. (1976) Purification and characterization of phosphoenolpyruvate carboxylase from maize leaves. Plant Physiol. 57, 906–910

    Google Scholar 

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Author information

Author notes
  1. C. A. Adams

    Present address: Department of Biology, Texas A & M University, 77843, College Station, TX, USA

Authors and Affiliations

  1. ARCO Plant Cell Research Institute, 6560 Trinity Ct., 94568, Dublin, CA, USA

    C. A. Adams, F. Leung & S. S. M. Sun

Authors
  1. C. A. Adams
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  2. F. Leung
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Adams, C.A., Leung, F. & Sun, S.S.M. Molecular properties of phosphoenolpyruvate carboxylase from C3, C3−C4 intermediate, and C4 Flaveria species. Planta 167, 218–225 (1986). https://doi.org/10.1007/BF00391418

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  • Received: 14 June 1985

  • Accepted: 19 September 1985

  • Issue date: February 1986

  • DOI: https://doi.org/10.1007/BF00391418

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Key words

  • C3−C4 intermediate
  • Flaveria
  • Phosphoenolpyruvate carboxylase isoenzymes
  • Photosynthesis (C3, C4, C3−C4)

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