Abstract
A study was made of the structure and function of senescent chloroplasts from a non-yellowing (NY) mutant of Festuca pratensis. Electron microscopy suggested that the stroma matrix was destroyed but that thylakoid membranes persisted in a loose, unstacked condition. By contrast, chloroplasts from the normal (Y) genotype lost both stroma and recognizable thylakoid systems. Fraction 1, the major protein of the stroma, disappeared from Y and NY at similar rates during senescence. The activities of photosystems I and II from NY also declined at a similar rate to Y photosystems. Polypeptides of chloroplast membranes were separated by SDS gel electrophoresis into at least 30 components. There was considerable heterogeneity in rates of breakdown of the different protein species of the membranes. Of the five major polypeptide components, two had kinetics of breakdown similar to those of stroma proteins and were lost from NY and Y at about the same rate, whereas the remaining three (one of which was tentatively identified as the apoprotein of the light-harvesting chlorophyll-protein complex) were more stable in NY than in Y. These results are discussed in relation to the mechanism and function of chloroplast disintegration during leaf senescence.
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Abbreviations
- RuDPC:
-
ribulose diphosphate carboxylase
- NY and Y:
-
non-yellowing and normal genotypes of Festuca, respectively
- PSI and PSII:
-
photosystems I and II, respectively
- SDS:
-
sodium dodecyl sulphate
- MW:
-
molecular weight
- CF:
-
coupling factor
References
Anderson, J.M.: The molecular organization of chloroplast thylakoids. Biochim. Biophys. Acta 416, 191–235 (1975)
Biswal, U.C., Mohanty, P.: Ageing induced changes in photosynthetic electron transport of detached barley leaves. Plant & Cell Physiol. 17, 323–331 (1976)
Butler, R.D., Simon, E.W.: Ultrastructural aspects of senescence in plants. Advanc. Gerontol. Res. 3, 73–129 (1970)
Fairbanks, G., Stech T., Wallach, D.: Electrophoretic analysis of the major polypeptides on the human erthrocyte membrane. Biochemistry 10, 2606–2617 (1971)
Henriques, F., Park, R.B.: Biosynthesis of grana and stroma lamellae in spinach. Plant Physiol. 54, 386–391 (1974)
Henriques, F., Park, R.B.: Further chemical and morphological characterization of chloroplast membranes from a chlorophyll b-less mutant of Hordeum vulgare. Plant Physiol. 55, 763–767 (1975)
Henriques, F., Park, R.B.: Identification of chloroplast membrane peptides with subunits of coupling factor and ribulose-1,5-diphosphate carboxylase. Arch. Biochem. Biophys. 176, 472–478 (1976a)
Henriques, F., Park, R.B.: Compositional characteritics of a chloroform-methanol soluble protein fraction from spinach chloroplast membranes. Biochim. Biophys. Acta 430, 313–320 (1976b)
Huffaker, R.C., Peterson, L.W.: Protein turnover in plants and possible means of its regulation. Ann. Rev. Plant Physiol. 25, 363–392 (1974)
Krupa, Z., Baszynski, T.: Requirement of galactolipids for photosystem I activity in lyophilized spinach chloroplasts. Biochim. Biophys. Acta 408, 26–34 (1975)
Lowry, O.H. rosebrough, N.J., Farr, A.L., Randall, R.J.: Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193, 266–275 (1951)
Lyttleton, J.W. Ts'o, P.O.P.: The localization of fraction I protein of green leaves in the chloroplasts. Arch. Biochem. Biophys. 73, 120–126 (1958)
MacKinney, G.: Criteria for purity of chlorophyll preparations. J. Biol. Chem. 132, 91–109 (1940)
Margulies, M.M.: Electron transport properties of chloroplasts from aged bean leaves and their relationship to the manganese content of the chloroplasts. In: Proc. 2nd Int. Congr. Photosynthesis Res., Stresa, Italy, 1, 539–545. The Hague: Dr. W. Junk NV Publishers 1971
Martin, C., Thimann K.V.: The role of protein synthesis in the senescence of leaves. I. The formation of protease. Plant Physiol. 49, 64–71 (1972)
Osmond, C.B.: Carbon reduction and photosystem II deficiency in leaves of C4 plants. Aust. J. Plant Physiol. 1, 41–50 (1974)
Peterson, L.W., Huffaker, R.C.: Loss of ribulose 1,5 diphosphate carboxylase and increase in proteolytic activity during senescence of detached primary barley leaves. Plant Physiol. 55, 1009–1015 (1975)
Reynolds, E.S.: The use of lead citrate at high pH as an electronopaque stain in electron microscopy. J. Cell Biol. 17, 208–212 (1963)
Spurr, A.R.: A low viscosity epoxy resin embedding medium for electron microscopy. J. Ultrastruct. Res. 26, 31–43 (1969)
Tetley, R.M., Thimann K.V.: The metabolism of oat leaves during senescence. I. Respiration, carbohydrate metabolism and action of cytokinins. Plant Physiol. 54, 294–303 (1974)
Thomas, H.: Regulation of alanine aminotransferase in leaves of Lolium temulentum during senescence. Z. Pflanzenphysiol. 74, 208–218 (1975a)
Thomas, H.: Leaf growth and senescence in grasses. Rep. Welsh Pl. Breed. Stn. for 1975, 133–138 (1975b)
Thomas, H.: Delayed senescence in leaves treated with the protein synthesis inhibitor MDMP. Plant Sci. Lett. 6, 369–377 (1976)
Thomas, H., Stoddart, J.L.: Separation of chlorophyll degradation from other senescence processes in leaves of a mutant genotype of meadow fescue (Festuca pratensis L). Plant Physiol. 56, 438–441 (1975)
Trebst, A.: Measurement of Hill reactions and photoreduction. Meth. Enzymol. 24, 146–165 (1972)
Uhrig, U., Tevini, M.: Effekte der Phospholipase D auf den Elektronentransport und die Lipidzusammensetzung isolierter Spinatchloroplasten. Planta (Berl.) 128, 173–178 (1976)
Wareing, P.F., Seth, A.K.: Ageing and senescence in the whole plant. Wiss. Z. Univ. Rostock, 16, 542–558 (1967)
Weber, K., Osborn, M.: The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244, 4406–4412 (1969)
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Thomas, H. Ultrastructure, polypeptide composition and photochemical activity of chloroplasts during foliar senescence of a non-yellowing mutant genotype of Festuca pratensis Huds.. Planta 137, 53–60 (1977). https://doi.org/10.1007/BF00394435
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DOI: https://doi.org/10.1007/BF00394435