Abstract
An electron microscopic investigation of fine structural changes in post-meristematic cotyledon mesophyll cells during the period of storage protein accumulation (16–32 d after pollination) showed that the rough ER, the Golgi apparatus and the developing vacuome are intimately involved in the formation of storage protein bodies (aleurone bodies). At the onset of storage protein accumulation (16–18 d after pollination) storage protein-like material appears within Golgi vesicles and preformed vacuoles. At a later stage (24 d after pollination) similar material can also be detected within vesicles formed directly by the rough endoplasmic reticulum (ER). It is concluded that there are two routes for storage protein transport from its site of synthesis at the ER to its site of accumulation in the vacuome. The first route involves the participation of dictyosomes while the second route bypasses the Golgi apparatus. It appears that the normal pathways of membrane flow in the development of central vacuoles in post-meristematic cells are used to deposit the storage protein within the protein bodies. Thus, the protein body can be regarded as a transient stage in the process of vacuome development of these storage cells.
Article PDF
Similar content being viewed by others
Avoid common mistakes on your manuscript.
Abbreviations
- ER:
-
endoplasmic reticulum
References
Bain, J.M., Mercer, F.V.: Subcellular organization of the developing cotyledons of Pisum sativum L. Aust. J. Biol. Sci. 19, 49–67 (1966)
Bajracharya, D., Schopfer, P.: Effect of light on the development of glyoxysomal functions in the cotyledons of mustard (Sinapis alba L.) seedlings. Planta 145, 181–186 (1979)
Berjak, P.: Lysosomal compartmentation: Ultrastructural aspects of the origin, development, and function of vacuoles in root cells of Lepidium sativum. Ann. Bot. 36, 73–81 (1972)
Bergfeld, R., Hong, Y.-N., Kühnl, T., Schopfer, P.: Formation of oleosomes (storage lipid bodies) during embryogenesis and their breakdown during seedling development in cotyledons of Sinapis alba L. Planta 143, 297–307 (1978)
Burr, B., Burr, F.A.: Zein synthesis in maize endosperm by polyribosomes attached to protein bodies. Proc. Natl. Acad. Sci. USA 73, 515–519 (1976)
Burr, B., Burr, F.A., Rubenstein, I., Simon, M.N.: Purification and translation of zein messenger RNA from maize endosperm protein bodies. Proc. Natl. Acad. Sci. USA 75, 696–700 (1978)
Chrispeels, M.J.: The role of the endoplasmic reticulum in the biosynthesis and transport of macromolecules in plant cells. In: International Cell Biology, 1976–1977 pp. 284–292, Brinkley, B.R., Porter, K.R., eds New York: The Rockefeller University Press 1977
Davey, J.E., Van Staden, J.: Ultrastructural aspects of reserve protein deposition during cotyledonary cell development in Lupinus albus. Z. Pflanzenphys. 89, 259–271 (1978)
Fisher, D.G., Evert, R.F.: Endoplasmic reticulum-dictyosome involvement in the origin of refractive spherules in sieve elements of Davallia fijiensis Hook. Ann. Bot. 43, 255–258 (1979)
Harris, N., Boulter, D.: Protein body formation in cotyledons of developing cowpea (Vigna unguiculata) seeds. Ann. Bot. 40, 739–744 (1976)
Harris, N., Juliano, B.O.: Ultrastructure of endosperm protein bodies in developing rice grains differing in protein content. Ann. Bot. 41, 1–5 (1977)
Khoo, U., Wolf, M.J.: Origin and development of protein granules in maize endosperm. Am. J. Bot. 57, 1042–1050 (1970)
Kirk, J.T.O., Pyliotis, N.A.: Cruciferous oilseed proteins: The protein bodies of Sinapis alba seed. Aust. J. Plant Physiol. 3, 731–746 (1976)
Kyle, D.J., Styles, E.D.: Development of aleurone and sub-aleurone layers in maize. Planta 137, 185–193 (1977)
Layne, E.: Spectrophotometric and turbidimetric methods for measuring proteins. In: Methods in Enzymology, vol. III, pp. 447–454, Colowick, S.P., Kaplan, N.O., eds. New York: Academic Press 1957
Marty, F.: Cytochemical studies on GERL, provacuoles, and vacuoles in root meristematic cells of Euphorbia. Proc. Natl. Acad. Sci. USA 75, 852–856 (1978)
Matile, P.: The lytic compartment of plant cells. Cell Biology Monographs, vol. 1. Wien, New York: Springer 1975
Millerd, A.: Biochemistry of legume seed proteins. Annu. Rev. Plant Physiol. 26, 53–72 (1975)
Neumann, D., Weber, E.: Formation of protein bodies in ripening seeds of Vicia faba L. Biochem. Physiol. Pflanzen 173, 167–180 (1978)
Nishizawa, N., Mori, S.: Vacuole formation by autophagy in the cortex cells of rice roots water-cultured with hemoglobin. J. Sci. Soil, Manure, Japan 48, 471–480 (1977)
Pernollet, J.-C.: Protein bodies of seeds: Ultrastructure, biochemistry, biosynthesis and degradation. Phytochemistry 17, 1473–1480 (1978)
Rest, J.A., Vaughan, J.G.: The development of protein and oil bodies in the seed of Sinapis alba L. Planta 105, 245–262 (1972)
Schopfer, P., Bajracharya, D., Plachy, C.: Control of seed germination by abscisic acid. I. Time course of action in Sinapis alba L. Plant Physiol. 64, 822–827 (1979)
Schopfer, P., Bergfeld, R., Kühnl, T.: Development of cytoplasmic organelles (aleurone bodies, oleosomes) from the endoplasmic reticulum in plants. In: Cell Compartmentation and Metabolic Channeling, pp. 345–357, Nover, L., Lynen, F., Mothes, K., eds. Proc. Leopoldina Sympos. Jena: Fischer, Amsterdam: North Holland Biomedical Press 1979
Walbot, V.: Control mechanisms for plant embryogeny. In: Dormancy and Developmental Arrest, pp. 113–166, Clutter, M.E., ed. New York: Academic Press 1978
Werker, E., Vaughan, J.G.: Anatomical and ultrastructural changes in aleurone and myrosin cells of Sinapis alba during germination. Planta 116, 243–255 (1974)
Werker, E., Vaughan, J.G.: Ontogeny and distribution of myrosin cells in the shoot of Sinapis alba L. A light- and electronmicroscope study. Isr. J. Bot. 25, 140–151 (1976)
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Bergfeld, R., Kühnl, T. & Schopfer, P. Formation of protein storage bodies during embryogenesis in cotyledons of Sinapis alba L.. Planta 148, 146–156 (1980). https://doi.org/10.1007/BF00386415
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00386415