Abstract
The amino acid (35S-methionine) incorporating activity of an in vitro wheat germ translation system was found to be maximal in 80 to 125 mol m−3 K with 2 to 4 mol m−3 Mg both as the acetate. Substitution of Na for K, or chloride for acetate at concentrations above 80 mol m−3 inhibited incorporation. When the K acetate concentration was raised to 200 mol m−3, no incorporation of radioactive methionine occurred.
Translation by polysomes extracted from leaf tissue of S. maritima, supplemented with postribosomal supernatant from wheat germ, showed activity which was optimal in the presence of 225 mol m−3 K acetate and 8 mol m−3 Mg acetate. However, the translation system was not directly comparable with the wheat germ system, as studies with an initiation inhibitor, aurintricarboxylic acid, suggested that the S. maritima system was essentially elongation-dependent, while initiation occurred in the wheat germ system.
Elongation-dependent polysomal preparations were extracted from leaves of the glycophytes Pisum sativum, Triticum aestivum, Oryza sativa and Hordeum vulgare, and from the halophytes Atriplex isatidea and Inula crithmoides. Translation by polysomes from the salt-tolerant plants was optimal at higher K and Mg concentrations, than by polysomes from the glycophytes. Furthermore, NaCl was better able partially to substitute for the role of K in polysomal preparations from halophytes than glycophytes.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Brady C J, Gibson T S, Barlow E W R, Speirs J and Wyn Jones R G 1984 Salt-tolerance in plants. I. Ions, compatible organic solutes and the stability of plant ribosomes. Plant. Cell Environ. 7, 571–578.
BRL 1981 BRL in vitro translation systems: Nuclease-treated and untreated wheat germ extract systems. Bethesda Research Laboratories. Gaithersburg, MD.
Carlier A R and Peumans W J 1976 The rye embryo system as an alternative to the wheat system for protein synthesis in vitro. Biochim. Biophys. Acta 447, 436–444.
Dalmond D 1988 The Effect of Ions on in vitro Protein Synthesis in the Halophyte Suaeda maritima. D. Ph. Thesis, University of Sussex, Brighton, UK.
Flowers T J 1985 Physiology of halophytes. Plant and Soil 89, 41–56.
Flowers T J and Hall J L 1978 Salt tolerance in the halophyte, Suaeda maritima (L.) Dum.: The influence of salinity of the culture solution on the content of various organic compounds. Ann. Bot. 42, 1057–1063.
Flowers T J, Troke P F and Yeo A R 1977 The mechanism of salt tolerance in halophytes. Annu. Rev. Plant Physiol. 28, 89–121.
Howers T J, Hajibagheri M A and Clipson N J 1986 Halophytes. Quart. Rev. Biol. 61, 313–337.
Gibson T S, Speirs J and Brady C J 1984 Salt tolerance in plants. II. In vitro translation of m-RNAs from salt-tolerant and salt-sensitive plants on wheat germ ribosomes: Responses to ions and compatible solutes. Plant, Cell Environ. 7, 579–587.
Gimmler H, Kaaden R, Kirchner U and Weyand A 1984 The chloride sensitivity of Dunaliella parva enzymes. Z. Pflanzenphysiol. 114, 131–150.
Hajibagheri M A, Yeo A R and Flowers T J 1985 Salt tolerance in Suaeda maritima (L.) Dum.: Fine structure and ion concentrations in the apical region of roots. New Phytol. 99, 331–343.
Hajibaheri M A and Flowers T J 1989 X-ray microanalysis of ion distribution within root cortical cells of the halophyte Suaeda maritima. Planta 177, 131–134.
Harvey D M R, Hall J L, Flowers T J and Kent B 1981 Quantitative ion localization within Suaeda maritima mesophyll cells. Planta 151, 555–560.
Igarashi K, Hashimoto S, Miyake A, Kashiwagi K and Hirose S 1982 Increase of fidelity of polypeptide synthesis by spermidine in eukaryotic cell-free systems. Eur. J. Biochem. 128, 597–604.
Konecki D, Kramer G, Pinphanichakarn P and Hardesty B 1975 Polyamines are necessary for maximum in vitro synthesis of globin peptides and play a role in chain initiation. Arch. Biochem. Biophys. 169, 192–198.
Marcu K and Duddock B 1974 Characterization of a highly efficient protein synthesizing system derived from commercial wheat germ. Nucl. Acids Res. 1, 1385–1397.
Markus A, Bewley J D and Weeks D P 1970 Aurintricarboxylic acid and initiation factors of wheat embryos. Science 167, 1735–1736.
Peumans W J, Carlier A R and Delaey B M 1980 Preparation and characterization of a highly active cell-free proteinsynthesizing system from dry pea primary axes. Plant Physiol. 66, 584–587.
Roberts B E and Paterson B M 1973 Efficient translation of tobacco mosaic virus RNA and rabbit globin 9S RNA in a cell-free system from commercial wheat germ. Proc. Natl. Acad. Sci. USA 70, 2330–2334.
Schleif R F and Wensink P C 1981 Practical Methods in Molecular Biology. pp 161–3. Springer-Verlag, Berlin.
Weber L A, Hickey E D, Maroney P A and Baglioni C 1977 Inhibition of protein synthesis by Cl-. J. Biol. Chem. 252, 4007–4010.
Wyn Jones R G, Brady C J and Speirs J 1979 Ionic and osmotic relations in plant cells. In Recent Advances in the Biochemistry of the Cereals, Annu. Proc. Phytochem. Soc. Eur. No. 16. Eds. D L Laidman and R G Wyn Jones. pp 63–104. Academic Press, London.
Yeo A R and Flowers T J 1980 Salt tolerance in the halophyte Suaeda maritima (L.) Dum.: Evaluation of the effect of salinity upon growth. J. Exp. Bot. 31, 1171–1183.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Flowers, T.J., Dalmond, D. Protein synthesis in halophytes: The influence of potassium, sodium and magnesium in vitro. Plant Soil 146, 153–161 (1992). https://doi.org/10.1007/BF00012008
Issue Date:
DOI: https://doi.org/10.1007/BF00012008