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Characterization of a novel barley β-amylase gene expressed only during early grain development

Published online by Cambridge University Press:  22 February 2007

Woosuk Jung*
Affiliation:
Department of Agronomy, University of Wisconsin-Madison, Madison, WI 53706;
Ronald W. Skadsen
Affiliation:
Cereal Crops Research Unit, USDA-ARS, 501 Walnut St., Madison, WI 53705, USA
David M. Peterson
Affiliation:
Department of Agronomy, University of Wisconsin-Madison, Madison, WI 53706; Cereal Crops Research Unit, USDA-ARS, 501 Walnut St., Madison, WI 53705, USA
*
*Correspondence Fax.: 301-504-5728 Email: [email protected]

Abstract

A developmentally regulated, novel β-amylase gene (ESDbamy) from Hordeum vulgare L. has 76% amino acid similarity with a previously described barley β-amylase. However, the 3' -end sequences of these β-amylases were different. The glycine-rich repeats, which are signature sequences of endosperm-type β-amylases, are absent in this novel ESDbamy gene. ESDbamy is highly expressed in the caryopsis during early development; however, it is not expressed in other tissues. Early seed development-specific (ESD) β-amylase mRNA levels and enzyme activities were higher in a shrunken endosperm mutant, seg8, than in the wild type. Seg8 has defective endosperm development, reduced starch synthesis and elevated monosaccharide concentrations

Type
Research Article
Copyright
Copyright © Cambridge University Press 2001

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References

Ainsworth, C.C., Miller, T.E. and Gale, M.D. (1987) α-Amylase and β-amylase homeoloci in species related to wheat. Genetical Research 49, 93103.CrossRefGoogle Scholar
Brown, R.C., Lemmon, B.E. and Olsen, O.-A. (1994) Endosperm development in barley: Microtubule involvement in the morphogenetic pathway. Plant Cell 6, 12411252.CrossRefGoogle ScholarPubMed
Daussant, J. and Laurière, C. (1990) Detection and partial characterization of two antigenically distinct β-amylases in developing kernels of wheat. Planta 181, 505511.CrossRefGoogle ScholarPubMed
Daussant, J., Zbaszyniak, B., Sadowski, J. and Wiatroszak, I. (1981) Cereal β-amylase: Immunochemical study on two enzyme-deficient inbred lines of rye. Planta 151, 176179.CrossRefGoogle Scholar
Daussant, J., Sadowski, J., Rorat, T., Mayer, C. and Laurière, C. (1991) Independent regulatory aspects and posttranslational modifications of two β-amylases of rye -use of a mutant inbred line. Plant Physiology 96, 8490.CrossRefGoogle ScholarPubMed
Djarot, I. N. and Peterson, D.M. (1991) Seed development in a shrunken endosperm barley mutant. Annals of Botany 68, 495499.CrossRefGoogle Scholar
Duffus, C.M. and Cochrane, M.P. (1992) Grain structure and composition. pp.291317in Shewry, P.R. (Ed.) Barley: Genetics, biochemistry, molecular biology and biotechnology. Wallingford, CAB International.Google Scholar
Gawel, N.J. and Jarret, R.L. (1991) A modified CTAB DNA extraction procedure for Musa and Ipomoea. Plant Molecular Biology Reporter 9, 262266.CrossRefGoogle Scholar
Giese, H. and Hejgaard, J. (1984) Synthesis of salt-soluble proteins in barley. Pulse-labeling study of grain filling in liquid-cultured detached spikes. Planta 161, 172177.CrossRefGoogle ScholarPubMed
Hejgaard, J. and Carlsen, S. (1977) Immunoelectrophoretic identification of a heterodimer β-amylase in extracts of barley grain. Journal of the Science of Food and Agriculture 28, 900904.CrossRefGoogle ScholarPubMed
Hildebrand, D.F. and Hymowitz, T. (1981) Role of β-amylase in starch metabolism during soybean seed development and germination. Physiologia Plantarum 53, 429434.CrossRefGoogle Scholar
Im, H. and Henson, C.A. (1995) Characterization of high pIα -glucosidase from germinated barley seeds: substrate specificity, subsite affinities and active-site residues. Carbohydrate Research 227, 145159.CrossRefGoogle Scholar
Jarvi, A.J. and Eslick, R.F. (1975) Shrunken endosperm mutants in barley. Crop Science 15, 363366.CrossRefGoogle Scholar
Jung, W., Skadsen, R.W. and Peterson, D.M. (1996) Characterization of a barley shrunken endosperm mutant, seg8. pp.505507in Slinkard, A.; Scoles, G.; Rossnagel, B. (Eds) V International oat conference and VII international barley genetics symposium: Proceedings. University of Saskatchewan, Saskatoon, Canada, University Extension Press.Google Scholar
Jung, W., Skadsen, R.W. and Peterson, D.M. (1997) Cloning and characterization of an early embryogenesis gene, EEA1 (Accession No. AF017430), from barley (PGR 97–184). Plant Physiology 115, 17301731.Google Scholar
Kreis, M., Williamson, M., Buxton, B., Pywell, J., Hejgaard, J. and Svendsen, I. (1987) Primary structure and differential expression of β-amylase in normal and mutant barleys. European Journal of Biochemistry 169, 517525.CrossRefGoogle ScholarPubMed
Kreis, M., Williamson, M.S., Shewry, P.R., Sharp, P. and Gale, M. (1988) Identification of a second locus encoding β-amylase on chromosome 2 of barley. Genetical Research 51, 1316.CrossRefGoogle Scholar
LaBerge, D.E. and Marchylo, B.A. (1983) Heterogeneity of the β-amylase enzymes of barley. Journal of the American Society of Brewing Chemists 41, 120124.CrossRefGoogle Scholar
LaBerge, D.E. and Marchylo, B.A. (1986) Changes in beta-amylase enzymes during kernel development of barley and the effect of papain as an extractant. Journal of the American Society of Brewing Chemists 44, 1619.CrossRefGoogle Scholar
MacGregor, A.W. and Dushnicky, L. (1989) α-Amylase in developing barley kernels—A reappraisal. Journal of the Institute of Brewing 95, 2933.CrossRefGoogle Scholar
McCleary, B.V. and Codd, R. (1989) Measurement of β-amylase in cereal flours and commercial enzyme preparations. Journal of Cereal Science 9, 1733.CrossRefGoogle Scholar
Mita, S., Suzuki-Fujii, K. and Nakamura, K. (1995) Sugar-inducible expression of a gene for β-amylase in Arabidopsis thaliana. Plant Physiology 107, 895904.CrossRefGoogle ScholarPubMed
Nakamura, K., Ohto, M., Yoshida, N. and Nakamura, K. (1991) Sucrose-induced accumulation of β-amylase occurs concomitant with the accumulation of starch and sporamin in leaf-petiole cuttings of sweet potato. Plant Physiology 96, 902909.CrossRefGoogle ScholarPubMed
Nitta, Y., Isoda, Y., Toda, H. and Sakiyama, F. (1989) Identification of glutamic acid 186 affinity-labeled by 2,3-epoxypropyl α-D-glucopyranoside in soybean β-amylase. Journal of Biochemistry 105, 573576.CrossRefGoogle ScholarPubMed
Nummi, M., Vilhunen, R. and Enari, T.M. (1966) β-Amylase: I. β-Amylases of different molecular size in barley and malt. pp.5261in European brewery convention. Proceedings of the 10thcongress, 1965, Stockholm, Sweden. Amsterdam, Elsevier Publishing Company.Google Scholar
Ohto, M., Nakamura-Kito, K. and Nakamura, K. (1992) Induction of expression of genes coding for sporamin and β-amylase by polygalacturonic acid in leaf-petiole cuttings of sweet potato. Plant Physiology 99, 422427.CrossRefGoogle ScholarPubMed
Ramage, R.T. and Crandall, C.L. (1981) Shrunken endosperm mutant seg8. Barley Genetics Newsletter 11, 34.Google Scholar
Rorat, T., Sadowski, J., Grellet, F., Daussant, J. and Delseny, M. (1991) Characterization of cDNA clones for rye endosperm β-amylase and analysis of β-amylase deficiency in rye mutant lines. Theoretical and Applied Genetics 83, 257263.CrossRefGoogle ScholarPubMed
Sadowski, J., Rorat, T., Cooke, R. and Delseny, M. (1993) Nucleotide sequence of a cDNA clone encoding ubiquitous β-amylase in rye (Secale cereale L.). Plant Physiology 102, 315316.CrossRefGoogle ScholarPubMed
Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular cloning, a laboratory manual (2nd edition). Cold Spring Harbor, NY, Cold Spring Harbor Laboratory Press.Google Scholar
Sanger, F., Nicklen, S. and Coulson, A.R. (1977) DNA sequencing with chain terminating inhibitors. Proceedings of the National Academy of Sciences, USA 74, 54635467.CrossRefGoogle ScholarPubMed
Shewry, P.R. (1993) Barley seed proteins. pp.131197 in MacGregor, A.W.; Bhatty, R.S. (Eds) Barley: Chemistry and technology. St. Paul, Minnesota, American Association of Cereal Chemists.Google Scholar
Shewry, P.R., Parmar, S., Buxton, B., Gale, M.D., Liu, C.J., Hejgaard, J. and Kreis, M. (1988) Multiple molecular forms of β-amylase in seeds and vegetative tissues of barley. Planta 176, 127134.CrossRefGoogle ScholarPubMed
Skadsen, R.W. (1993) Aleurones from a barley with low β-amylase activity become highly responsive to gibberellin when detached from the starchy endosperm. Plant Physiology 102, 195203.CrossRefGoogle Scholar
Sopanen, T. and Laurière, C. (1989) Release and activity of bound β-amylase in a germinating barley grain. Plant Physiology 89, 244249.CrossRefGoogle Scholar
Sun, Z. and Henson, C.A. (1991) A quantitative assessment of the importance of barley seed α-amylase, β-amylase, debranching enzyme, and α-glucosidase in starch degradation. Archives of Biochemistry and Biophysics 284, 298305.CrossRefGoogle ScholarPubMed
Tibbot, B.K. and Skadsen, R.W. (1996) Molecular cloning and characterization of a gibberellin-inducible, putative α-glucosidase gene from barley. Plant Molecular Biology 30, 229241.CrossRefGoogle ScholarPubMed
Toda, H., Nitta, Y., Asanami, S., Kim, J. and Sakiyama, F. (1993) Sweet potato β-amylase primary structure and identification of the active-site glutamyl residue. European Journal of Biochemistry 216, 2538.CrossRefGoogle ScholarPubMed
Wang, S.M., Lue, W.L., Eimert, K. and Chen, J. (1996) Phytohormone-regulated β-amylase gene expression in rice. Plant Molecular Biology 31, 975982.CrossRefGoogle ScholarPubMed
Wang, S.M., Lue, W.L., Wu, S.Y., Huang, H.W. and Chen, J. (1997) Characterization of a maize β-amylase cDNA clone and its expression during seed germination. Plant Physiology 113, 403409.CrossRefGoogle ScholarPubMed
Wesenberg, D.M., Hayes, R.M., McKay, H.C., Standridge, N.N., Goplin, E.D. and Petr, F.C. (1974) Registration of Klages barley. Crop Science 14, 337338.CrossRefGoogle Scholar
Yoshigi, N., Sahara, H. and Koshino, S. (1995) Role of the C-terminal region of β-amylase from barley. Journal of Biochemistry 117, 6367.CrossRefGoogle ScholarPubMed
Ziegler, P. (1999) Cereal beta-amylases. Journal of Cereal Science 29, 195204.CrossRefGoogle Scholar