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Changes in protein synthesis in embryonic axes after long-term storage of maize seeds

Published online by Cambridge University Press:  19 September 2008

R. Aguilar ,
E. Reynoso ,
M. Albores  and
E. Sánchez de Jiménez
R. Aguilar
Affiliation:
Department of Biochemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
E. Reynoso
Affiliation:
Department of Organic Chemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
M. Albores
Affiliation:
Department of Organic Chemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
E. Sánchez de Jiménez*
Affiliation:
Department of Biochemistry, Facultad de Química, UNAM, Ciudad Universitaria, Mexico D F, 04510Mexico
*
* Correspondence
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Abstract

The aim of this work was to analyse the capacity for protein synthesis in embryonic axes from long-term-stored maize seeds, including the role of proline. Embryonic axes from seeds stored for 13 years (S) and non-stored seeds (NS) were incubated in nutrient media after application of [14C]proline. Transformation of [14C]proline into other amino acids was analysed by thin-layer chromatography. After 6 h of incubation, no other labelled amino acids were found. Incorporation of 14C into total soluble and cell-wall (proline-rich) proteins was assessed during this period. Incorporation of [14C]proline into specific cell-wall proteins was lower in S than in NS axes.

Studies using [35S]methionine showed that protein synthesis was slower in axes of S than in NS seeds. Analyses of these proteins by gel electrophoresis and fluorography revealed qualitative differences between the [35S]methionine proteins synthesized by both types of axes. The NS: S ratios for the [35S]proteins were larger than those from the [14C]proline assays. These data may be interpreted as an indication of differential deterioration of transcription or translation in the axes during long-term seed storage.

Keywords

prolineprotein synthesisseed storageZea mays
Type
Research Papers
Information
Seed Science Research , Volume 2 , Issue 4 , December 1992 , pp. 191 - 198
Copyright
Copyright © Cambridge University Press 1992

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References

Abernethy, R.H., Thiel, D.S., Petersen, N.S. and Helm, K. (1989) Thermotolerance is developmentally dependent in germinating wheat seed. PlantPhysiology 89, 569–576.Google ScholarPubMed
Abdul-Baki, A.A. (1980) Biochemical aspects of seed vigor.HortScience 15, 765–771.CrossRefGoogle Scholar
Aguilar, R. and Sánchez de Jiménez, E. (1984) Aminoacid pools and protein synthesis in germinating maize embryos. Plant Cell Reports 3, 193–195.CrossRefGoogle Scholar
Averyhart-Fullard, V., Datta, K. and Marcus, A. (1988) A hydroxy proline-rich protein in the soybean cell wall. Proceedings of the NationalAcademy of Science USA 85, 1082–1085.CrossRefGoogle Scholar
Bates, L.S., Waldrev, R.P. and Teare, I.D. (1973) Rapid determination of free proline for water stress studies. Plant and Soil 39, 205–207.CrossRefGoogle Scholar
Bonner, W.M. and Laskey, R.A. (1974) A film detection method for tritium-labeled protein and nucleic acids in polyacrylamide gels. European Journal of Biology 46, 83–88.CrossRefGoogle Scholar
Bray, G.A. (1960) A simple efficient liquid scintillator for counting aqueous solutions in a liquid scintillation counter. Analytical Biochemistry 1, 229–235.CrossRefGoogle Scholar
Chrispeels, M.J., Sadava, D. and Cho, Y.P. (1974) Enhancementof extensin biosynthesis in ageing disks of carrot storage tissue. Journal of Experimental Botany 25, 1157–1166.CrossRefGoogle Scholar
Cooper, J.B. and Varner, J.E. (1983) MSelective inhibition of proline hydroxylation by 3,4-dehydroproline. Plant Physiology 73,324–328.CrossRefGoogle Scholar
Datta, K., Schmidt, A. and Marcus, A. (1989) Characterization of two soybean repetitive proline-rich proteins and a cognate cDNA from germinated axes. Plant Cell 1, 945–952.Google Scholar
,Dell'Aquila, A. (1987) Mean germination time as a monitor of the seed ageing. Plant Physiology and Biochemistry 25, 761–768.Google Scholar
Helm, K.W. and Abernethy, H. (1990) Heat shock proteins and their mRNAs in dry and early imbibing embryos of wheat. Plant Physiology 93, 1626–1633.CrossRefGoogle ScholarPubMed
Hong-qui, Z. and Croes, A.F. (1983) Proline metabolism in pollen: degradation of proline during germination and early tube growth. Planta 159, 46–49.CrossRefGoogle Scholar
Hood, E.E., Chen, Q.X. and Varner, J.E. (1988) A developmentally regulated hydroxyproline-rich glycoprotein in maize pericarp cell walls. Plant Physiology 87, 138–142.CrossRefGoogle ScholarPubMed
Kermode, R.A. (1990) Regulatory mechanism involved in the transition from seed development to germination. Critical Review in Plant Sciences 9, cap 2, 155–195.CrossRefGoogle Scholar
Kermode, R.A., Bewley, J.D., Dasgupta, J. and Misra, S. (1986) The transition from seed development to germination: a key role for desiccation? HortScience 25, (5) 1113–1118.CrossRefGoogle Scholar
José-Estanyol, M., Ruiz-Avila, L. and Puigdoménech, P. (1992) A maize embryo specific gene encodes a proline-rich and hydrophobic protein. Plant Cell 4, 413–423.Google ScholarPubMed
Laemmli, U.K. (1970) Cleavage of structural proteins during theassembly of the head of bacteriophage T4. Nature 227, 680–685.CrossRefGoogle ScholarPubMed
Lowry, O.H., Rosebrough, N., Farr, A. and Randall, R.J. (1951) Protein measurements with the folin-phenol reagent. Journal of Biological Chemistry 193, 265–275.CrossRefGoogle ScholarPubMed
Mayer, L.M. and Poljakoff-Mayber, A. (1989) The germinationof seeds. Oxford, Pergamon.Google Scholar
O'Farrell, P.H. (1975) High resolution two dimensional electrophoresis of protein. Journal of Biological Chemistry 250, 4007–4021.CrossRefGoogle Scholar
Parmeggiani, A., Singer, C. and Gottsochalk, (1971) Purification of the amino acid polymerization factors from Escherichia coli. pp. 291–302 in Colowick, S.P. and Kaplan, N.O. (Eds) Methods inenzymology. New York, Academic Press.Google Scholar
Pérez, L., Aguilar, R. and Sánchez de Jiménez, E. (1987) Effect of an exogenous auxin on maize tissues. Alteration of protein synthesis and phosphorylation. Physiologia Plantarum 69, 517–522.CrossRefGoogle Scholar
Ruiz-Avila, L.:, Ludevid, D.M. and Puigdoménech, P. (1991) Differential expression of a hydroxyproline-rich cell-wall protein in embryonic tissues of Zea mays. Planta 184, 130–136.CrossRefGoogle ScholarPubMed
Smith, C.A.D. and Bray, C.M. (1984) Polyadenylated RNA levels and macromolecular synthesis during loss of seed vigour. Plant Science Letters 34, 335–343.CrossRefGoogle Scholar
Smith, I. (1968) Zone electrophoresis. p. 166 in Smith, I. (Ed.) Chromatographic and electrophoretic techniques, vol. 2. New York, John Wiley & Sons.Google Scholar
Zheng-Hua, Y. and Varner, J.G. (1991). Tissue-specific expression of cell wall proteins in developing soybean tissues. Plant Cell 3, 23–37.Google Scholar