Abstract
The flag leaf of wheat was examined for changes in quantity and activity of ribulose-bisphosphate carboxylase (RuBPCase; EC 4.1.1.39), in the proteolytic degradation of RuBPCase and other native proteins, and in the ultrastructure of the leaf cells during grain development. Proteolytic degradation of RuBPCase at pH 4.8 increased until 8–10 d after anthesis, then declined, and increased again 16–18 d after anthesis. The second peak coincided with the onset of a preferential loss of immunologically recognizable RuBPCase. The specific activity and number of active sites per molecule of RuBPCase did not change during senescence. Examination of ultrastructure with the electron microscope showed little change in the appearance of the mitochondria as the flag leaf aged. Prominent cristae were still evident 35 d after anthesis. In contrast, the chloroplasts showed a progressive disruption of the thylakoid structure and an increasing number of osmiophilic glubules. The double membrane envelope surrounding the chloroplast appeared intact until at least 20 d after anthesis. The tonoplast also appeared intact up to 20 d. At later stages of senescence of the leaf the outer membrane of the chloroplast adjacent to the tonoplast appeared to break but the inner membrane of the envelope appeared intact until at least 35 d after anthesis.
Similar content being viewed by others
Abbreviations
- RuBPCase:
-
ribulose-1,5-bisphosphate carboxylase (EC. 4.1.1.39)
References
Barr, R., Arntzen, C.J. (1969) The occurrence of S-tocopheryl quinone in higher plants and its relation to senescence. Plant Physiol 44, 591–598
Barton, R. (1966) Fine structure of mesophyll cells in senescing leaves of Phaseolus. Planta 71, 314–325
Brady, C.J., Patterson, B.D., Tung, H.F., Smillie, R.M. (1971) Protein and RNA synthesis during ageing of chloroplasts in wheat leaves. In: Autonomy and biogenesis of mitochondria and chloroplasts, pp. 453–465, Boardman, N.K., Linnane, A.W., Smillie R.M., eds. North-Holland Publishing Co., Amsterdam
Butler, R.D. (1967) The fine structure of senescing cotyledons of cucumber. J. Exp. Bot 18, 535–543
Butler, R.D., Simon, E.W. (1971) Ultrastructural aspects of senescence in plants. In: Advance in geronotological research, vol. 3, pp. 73–129, Strehler, B.L., ed. Academic Press, New York
Callow, J.A. (1974) Ribosomal RNA, fraction 1 protein synthesis, and ribulose diphosphate carboxylase activity in developing and senescing leaves of cucumber. New Phytologis 73, 13–20
Dalling, M.J., Boland, G., Wilson, J.H. (1976) Relation between acid proteinase activity and redistribution of nitrogen during grain development in wheat. Aust. J. Plant Physiol. 3, 721–730
Dennis, D.T., Stubbs, M., Coultake, T.P. (1967) The inhibition of brussels sprout leaf senescence by kinins. Can. J. Bot. 45, 1019–1024
Frith, G.J.T., Dalling, M.J. (1980) The role of peptide hydrolases in leaf senescence. In: Methods of aging research, vol. II, Senescence in plants, Thimann, K.V., ed. (in press) CRC Press, West Palm Beach, Fla., USA
Gordon, K.H.J., Peoples, M.B., Murray, D.R. (1978) Ageing-linked changes in photo synthetic capacity and in fraction 1 protein content of the first leaf of pea Pisum sativum L. New Phytologist 81, 35–42
Gornall, A.G., Bardawill, C.J., David, M.M. (1949) Determination of serum proteins by means of the biuret reaction. J. Biol. Chem. 177, 751–766
Hall, A.J., Brady, C.J. (1977) Assimilate source-sink relationships in Capsicum annuum L. II. Effects of fruiting and defloration on the photosynthetic capacity and senescence of the leaves. Aust. J. Plant Physiol. 4 771–783
Hall, N.P., Keys, A.J., Merrett, M.J. (1978) Ribulose 1,5-diphosphate carboxylase protein during flag leaf senescence. J. Exp. Bot. 29, 31–37
Huffaker, R.C., Miller, B.L. (1978) Reutilization of ribulose bisphosphate carboxylase. In: Brookhaven Symp. in Biol. No. 30, On photosynthetic carbon assimilation, pp. 139–152, Siegelman, H.W., Hind, G. eds. New York, N.Y., USA Plenum Publishing Corp.
Hurkman, W.J. (1979) Ultrastructural changes of chloroplasts in attached and detached, aging primary wheat leaves. Am. J. Bot. 66, 64–70
Jensen, R.G., Bahr, J.T. (1977) Ribulose 1,5-bisphosphate carboxylase-oxygenase. Ann. Rev. Plant. Physiol. 28, 379–400
Kawashima, N., Mitake, T. (1969) Studies on protein metabolism in higher plants. IV. Changes in ribulose diphosphate carboxylase activity and fraction 1 protein content in tobacco leaves with age. Agr. Biol. Chem. 33, 539–543
Laurière, C., Skakoun, A., Daussant, J. (1975) Adaption of immunological methods to the study of ontogeny of proteins: Fraction 1 protein and malate dehydrogenase from senescing leaves of wheat. Physiol. Vég. 13, 467–478
Lawton, J.R., Harris, P.J. (1978) Fixation of senescing plant tissues: sclerenchymatous fibre cells from the flowering stem of a grass. J. Microscopy 112, 307–318
Lorimer, G.H., Badger, M.R., Andrews, T.J. (1977) D-Tibulose-1,5-bisphosphate carboxylase-oxygenase. Improved methods for the activation and assay of catalytic activities. Anal. Biochem. 78, 66–75
Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J. (1951) Protein measurement with the folin phenol reagent. J. Biol. Chem. 193, 265–272
Miziorko, H.M. (1979) Ribulose-1,5-bisphosphate carboxylase. Evidence in support of the existence of distinct CO2 activator and CO2 substrate sites. J. Biol. Chem. 254, 270–272
Paulsen, J.M., Lane, M.D. (1966) Spinach ribulose diphosphate carboxylase. I. Purification and properties of the enzyme. Biochemistry 5, 2350–2357
Peoples, M.B. (1980) Investigation of the degradative processes involved in the turn-over of ribulose 1,5-bisphosphate carboxylase in wheat leaves. University of Melbourne, Ph. D. Thesis Australia
Peoples, M.B., Dalling, M.J. (1978) Degradation of ribulose-1,5-bisphosphate carboxylase by proteolytic enzymes from crude extracts of wheat leaves. Planta 138, 153–160
Peoples, M.B., Dalling, M.J. (1979) Intracellular localization of acid peptide hydrolases in wheat leaves. (Abstr.) Plant Physiol. [Suppl.] 63, 159
Peoples, M.B., Frith, G.J.T., Dalling, M.J. (1979) Proteolytic enzymes in green wheat leaves. IV. Degradation of ribulose 1,5-bisphosphate carboxylase by acid proteinases isolated on DEAE-cellulose. Plant Cell Physiol. 20, 253–258
Peterson, L.W., Huffaker, R.C. (1975) Loss of ribulose 1,5-diphosphate carboxylase and increase in proteolytic activity during senescence of detached primary barley leaves. Plant Physiol. 55, 1009–1015
Peterson, L.W., Kleinkopf, G.E., Huffaker, R.C. (1973) Evidence for lack of turn-over of ribulose 1,5-diphosphate carboxylase in barley leaves. Plant Physiol. 51, 1042–1045
Regetli, H.W.J., Weintraub, M., Lo, E. (1970) Degeneration of leaf cells resulting from starvation after excision. I. Electron microscopic observation. Can. J. Bot. 48, 1913–1922
Salema, R., Brandao, I. (1973) The use of PIPES buffer in the fixation of plant cells for electron microscopy. J. Submier. Cytol. 5, 79–96
Shaw, M., Manocha, M.S. (1965) Fine structure in detached senescing wheat leaves. Can. J. Bot. 43, 747–755
Siegel, M.I., Lane, M.D. (1972) Interaction of ribulose diphosphate carboxylase with 2-carboxy-ribitol diphosphate, an analogue of the proposed carboxylated intermediate in the CO2 fixation reaction. Biochem. Biophys. Res. Commun. 48, 508–516
Siegel, M.I., Lane, M.D. (1973) Chemical and enzymatic evidence for the participation of a 2-carboxy-3-ketoribitol-1,5-diphosphate intermediate in the carboxylation of ribulose 1,5-diphosphate. J. Biol. Chem. 248, 5486–5498
Spurr, A.R. (1969) A low-viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 26, 31–43
Venable, J.H., Coggleshall, R. (1965) A simplified lead citrate stain for use in electron microscopy. J. Cell Biol. 25, 407–408
Waters, S.P., Peoples, M.B., Simpson, R.J., Dalling, M.J. (1980) Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). I. Peptide hydrolase activity and protein break-down in the flag leaf, glumes and stem. Planta 148, 422–428
Wishnick, M., Lane, M.D. (1969) Inhibition of ribulose disphosphate carboxylase by cyanide. J. Biol. Chem. 244, 55–59
Wishnick, M., Lane, M.D., Scrutton, M.C. (1970) The interaction of metal ions with ribulose 1,5-diphosphate carboxylase from spinach. J. Biol. Chem. 245, 4935–4947
Wittenbach, V.A. (1978a) Breakdown of ribulose bisphosphate carboxylase and change in proteolytic activity during dark-induced senescence in wheat seedlings. Plant Physiol. 62, 604–608
Wittenbach, V.A. (1978b) Changes in proteolytic activity and the level of RuBPCase in the flag leaf of wheat during grain development and senescence (Abstr.). Plant Physiol. [Suppl.] 61, 25
Wittenbach, V.A. (1979) Ribulose bisphosphate carboxylase and proteolytic activity in wheat leaves from anthesis through senescence. Plant Physiol 64, 884–887
Yemm, E.W., Cocking, E.C. (1955) The determination of amino acids with ninhydrin. Analyst 80, 209–213
Author information
Authors and Affiliations
Additional information
I=Waters et al. 1980
Rights and permissions
About this article
Cite this article
Peoples, M.B., Beilharz, V.C., Waters, S.P. et al. Nitrogen redistribution during grain growth in wheat (Triticum aestivum L.). Planta 149, 241–251 (1980). https://doi.org/10.1007/BF00384560
Received:
Accepted:
Issue Date:
DOI: https://doi.org/10.1007/BF00384560