Skip to main content
SpringerLink
Log in

Prolamellar bodies of oat, wheat, and rye: Structure, lipid composition, and adsorption of saponins

  • Published:
Protoplasma Aims and scope Submit manuscript

Summary

Membranolytic active saponins (26-desglucoavenacosides) derived from isolated oat-avenacosides adsorb to oat prolamellar bodies (PLBs), but not to wheat or rye etioplast inner membranes. Thus, the saponin adsorption is a peculiarity of oat PLBs but not a general tool for PLB-analysis. The qualitative and quantitative analysis of free sterols and galactolipids of isolated PLBs did not explain the exclusive adsorption of saponins to oat PLBs. In addition, isolated PLBs and prothylakoids (PTs) of all three plants did not differ with respect to the molecular species composition of mono- (MGDG) or di-galactosyldiacylglyceride (DGDG). Recrystallization leading to a structural reorganization of wheat PLBs (wide type to narrow type) also had no influence on the molecular species composition of the isolated etioplast inner membranes. These observations as well as earlier investigations raise the question, whether the composition of PLBs is responsible for the tubular, semicrystalline construction. Experiments with the chelating agent EDTA indicate an external influence on the PLB construction and underline the idea that the PLB construction is not influenced by the membrane components themselves. Low concentrations of EDTA in the isolation media decompose the paracrystalline structure of the PLBs into membranes, resembling those of greening plastids. Based on these experiments we assume the ionic environment in plastids to be responsible for the construction and decomposition of PLBs and that changes of the membrane components are of minor importance.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

Abbreviations

26-DGA:

26-desglucoavenacosides

BSA:

bovine serum albumine

DGDG:

digalactosyldiacylglyceride

HPLC:

high performance liquid chromatography

MGDG:

monogalactosyldiacylglyceride

PC:

phosphatidylcholine

PCR:

protochlorophyllide oxidoreductase

PLB:

prolamellar body

Pt:

prothylakoid

References

  • Berry DR, Smith H (1971) Red-light stimulation of prolamellar body recrystallization and thylakoid formation in barley etioplasts. J Cell Sci 8: 185–200

    Google Scholar 

  • Brandt R, Benveniste P (1972) Isolation and identification of sterols from subcellular fractions of bean leaves (Phaseolus vulgaris). Biochem Biophys Acta 282: 85–92

    Google Scholar 

  • Brangeon J (1974) Structural modifications in the lamellar system of isolatedZea mays chloroplasts under different ionic conditions. J Microscopie 21: 75–84

    Google Scholar 

  • Dehesh K, Ryberg M (1985) The NADPH-protochlorophyllide oxidoreductase is the major protein constituent of prolamellar bodies in wheat (Triticum aestivum L.). Planta 164: 396–399

    Google Scholar 

  • Elias PM, Friend DS, Goerke J (1979) Membrane sterol heterogenity. J Histochem Cytochem 27: 1247–1260

    Google Scholar 

  • Fukuda K, Utsumi H, Shoji J, Hamada A (1985) Saponins can cause the agglutination of phospholipid vesicles. Biochem Biophys Acta 820: 199–206

    Google Scholar 

  • Grünweller S, Kesselmeier J (1985) Characterization of a membrane bound β-glucosidase responsible for the activation of oat leaf saponins. Phytochemistry 24: 1941–1943

    Google Scholar 

  • Gunning BES (1965) The greening process in plastids. 1. The structure of the prolamellar body. Protoplasma 60: 112–130

    Google Scholar 

  • Henningsen KW, Boynton JE (1969) Macromolecular physiology of plastids. VII. The effect of brief illumination on plastids of dark-grown barley leaves. J Cell Sci 5: 757–793

    Google Scholar 

  • Ikeuchi M, Murakami S (1983) Separation and characterization of prolamellar bodies and prothylakoids from squash etioplasts. Plant Cell Physiol 24: 71–80

    Google Scholar 

  • Kanangara CG, Gough SP, Hansen B, Rasmussen JN, Simpson DJ (1977) A homogenizer with replaceable razor blades for bulk isolation of active barley plastids. Carlsberg Res Comm 42: 431–439

    Google Scholar 

  • Kesselmeier J (1982) Steroidal saponins in etiolated, greening and green leaves and in isolated etioplasts and chloroplasts ofAvena sativa. Protoplasma 112: 127–132

    Google Scholar 

  • —,Eichenberger W, Urban B (1985) High performance liquid chromatography of molecular species from free sterols and sterylglycosides isolated from oat leaves and seeds. Plant Cell Physiol 26: 463–471

    Google Scholar 

  • —,Heinz E (1985) Separation and quantisation of molecular species from plant lipids by high performance liquid chromatography. Anal Biochem 144: 319–328

    Google Scholar 

  • —,Laudenbach U (1986) Prolamellarbody structure, composition of molecular species and amount of galactolipids in etiolated, greening and reetiolated primary leaves of oat, wheat and rye. Planta 168: 453–460

    Google Scholar 

  • —,Schäfer B, Laudenbach U (1987) Changes of the galactolipid composition during illumination of isolated oat etioplasts. Plant Cell Physiol 28: 123–130

    Google Scholar 

  • —,Strack D (1981) High performance liquid chromatographíc analysis of steroidal saponins fromAvena sativa L. Z Naturforsch 36c: 1072–1074

    Google Scholar 

  • —,Urban B (1983) Subcellular localization of saponins in green and etiolated leavens and in green protoplasts of oat (Avena sativa L.). Protoplasma 114: 133–140

    Google Scholar 

  • Le-Quoc K, Le-Quoc D, Pugin A (1987) An efficient method for plant vacuole isolation using digitonin for plasmalemma lysis. J Plant Physiol 126: 329–335

    Google Scholar 

  • Lichtenthaler HK, Wellburn AR (1983) Determinations of total carotenoids and chlorophylls a and b of leaf extracts in different solvents. Biochem Soc Trans 603: 591–592

    Google Scholar 

  • Lütz C, Nordmann U (1983) The localization of saponins in prolamellar bodies mainly depends on the isolation of etioplasts. Z Pflanzenphysiol 110: 201–210

    Google Scholar 

  • — —,Tönissen H, Bergweiler P, Röper U (1984) On the lipid like character of prolamellar bodies. In:Sybesma C (ed) Advances in photosynthesis research, vol 4. Martinus Nijhoff/Dr. W. Junk Publishers, The Hague, pp 627–631

    Google Scholar 

  • Murakami S, Miyao M, Ikeuchi M (1983) Prolamellar body and saponins: Avenacosides are not constituents ofAvena etioplasts. Plant Cell Rep 2: 148–151

    Google Scholar 

  • —,Packer L (1971) The role of cations in the organization of chloroplast membranes. Arch Biochem Biophys 146: 337–347

    Google Scholar 

  • —,Yamada N, Nagano M, Osumi M (1985) Three dimensional structure of the prolamellar body in squash etioplasts. Protoplasma 128: 147–156

    Google Scholar 

  • Rascio N, Orsenigo M, Arboit D (1976) Prolamellar body transformation with increasing cell age in the maize leaf. Protoplasma 90: 253–263

    Google Scholar 

  • Ryberg M, Dehesh K (1986) Localization 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

    Google Scholar 

  • —,Sundqvist C (1982) Characterization of prolamellar bodies and prothylakoids fractionated from wheat etioplasts. Physiol Plant 6: 125–132

    Google Scholar 

  • —,Sandelius AS, Selstam E (1983) Lipid composition of prolamellar bodies and prothylakoids of wheat etioplasts. Physiol Plant 57: 555–560

    Google Scholar 

  • Schlösser E (1972) Sterol dependent membranelytic action of saponins. Phytopathol Z 74: 91–94

    Google Scholar 

  • Seemann P, Cheng D, Iles GH (1973) Structure of membrane holes in osmotic and saponin hemolysis. J Cell Biol 56: 519–527

    Google Scholar 

  • Seltsam E, Widell A, Johansson LBA (1987) A comparison of prolamellar bodies from wheat, Scots pine and Jeffrey pine. Pigment spectra and properties of protochlorophyllide oxidoreductase. Physiol Plant 70: 209–214

    Google Scholar 

  • Urban B, Laudenbach U, Kesselmeier J (1983) Saponin distribution in the etiolated leaf tissue and subcellular localization of steroidal saponins in etiolated protoplasts of oat (Avena sativa L.). Protoplasma 118: 121–123

    Google Scholar 

  • Wehrmeyer W (1965 a) Zur Kristallgitterstruktur der sogenannten Prolamellarkörper in Proplastiden etiolierter Bohnen. I. Pentagondodekaeder als Mittelpunkt konzentrischer Prolamellarkörper. Z Naturforsch 20b: 1270–1278

    Google Scholar 

  • — (1965 b) Zur Kristallgitterstruktur der sogenannten Prolamellarkörper in Proplastiden etiolierter Bohnen. II. Zinkblendegitter als Muster tubulärer Anordnung in Prolamellarkörpern. Z Naturforsch 20b: 1278–1288

    Google Scholar 

  • — (1965 c) Zur Kristallgitterstruktur der sogenannten Prolamellarkörper in Proplastiden etiolierter Bohnen. Wurzittgitter als Muster tubulärer Anordnung in Prolamellarkörpern. Z Naturforsch 20b: 1288–1296

    Google Scholar 

  • Wellburn AR, Quail PH, Gunning BES (1977) Examination of ribosome-like particles in isolated prolamellar bodies. Planta 134: 45–52

    Google Scholar 

Download references

Author information

Author notes

  1. J. Kesselmeier

    Present address: Abteilung Biogeochemie, Max-Planck-Institut für Chemie, Saarstrasse 23, D-6500, Mainz, Germany

Authors and Affiliations

  1. Botanical Institute, University of Cologne, Cologne

    G. Protoschill-Krebs & J. Kesselmeier

Authors
  1. G. Protoschill-Krebs
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. J. Kesselmeier
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Protoschill-Krebs, G., Kesselmeier, J. Prolamellar bodies of oat, wheat, and rye: Structure, lipid composition, and adsorption of saponins. Protoplasma 146, 1–9 (1988). https://doi.org/10.1007/BF01354289

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01354289

Keywords

Search

Navigation