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Molecular studies on osmoprimed seeds of cauliflower: a partial amino acid sequence of a vigour-related protein and osmopriming-enhanced expression of putative aspartic protease

Published online by Cambridge University Press:  19 September 2008

Yuzo Fujikura  and
Cees M. Karssen
Yuzo Fujikura*
Affiliation:
Department of Plant Physiology, Agricultural University, Arboretumlaan 4, 6703 BD, Wageningen, Netherlands
Cees M. Karssen
Affiliation:
Department of Plant Physiology, Agricultural University, Arboretumlaan 4, 6703 BD, Wageningen, Netherlands
*
*Correspondence
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Abstract

A partial amino acid sequence of a vigour-related protein, V-1, from cauliflower (Brassica oleracea L.) seeds was obtained, after isolation by two-dimensional gel electrophoresis and gas-phase micro-sequencing. The sequence was found to have high homology to soybean seed maturation proteins. However, the position of the sequence in the V-1 polypeptide suggests that the V-1 and soybean proteins have different polypeptide structures. An osmoprimed seeds cDNA library was constructed and has been screened by a cDNA probe derived from the V-1 sequence. Two cDNA clones with high homology to aspartic protease (EC 3.4.23) from barley grain were isolated. The expression of putative aspartic protease mRNA was found to be enhanced by osmopriming, however the clones were found to have no significant sequence homology to the V-1.

Keywords

aspartic proteaseBrassica oleracea L.cauliflowercDNAgerminationosmoprimingseed
Type
Short Communication
Information
Seed Science Research , Volume 5 , Issue 3 , September 1995 , pp. 177 - 181
Copyright
Copyright © Cambridge University Press 1995

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Footnotes

1

Present address: Institute of Experimental Botany, Czech Academy of Sciences, Sokolovska 6, 77200 Olomouc, Czech Republic.

References

Baker, J., Steele, C. and Dure, L. III,. (1988) Sequence and characterization of 6 Lea proteins and their genes from cotton. Plant Molecular Biology 11, 277–281.CrossRefGoogle ScholarPubMed
Cordeiro, M.C., Xue, Z.T., Pietrzak, M., Pais, M.S. and Brodelius, P.E. (1994) Isolation and characterization of a cDNA from flowers of Cynara cardunculus encoding cyprosin (an aspartic proteinase) and its use to study the organ-specific expression of cyprosin. Plant Molecular Biology 24, 733–741.Google Scholar
De Vries, S., Hoge, H. and Bisseling, T. (1988) Isolation of total and polysomal RNA from plant tissues. B6: 1–13 in Gelvin, S.B., Schilperoort, R.A. and Verma, D.P.S. (Eds) Plant molecular biology manual. Dordrecht, Kluwer Academic Publishers.Google Scholar
Faust, P.L., Kornfield, S. and Chirgwin, J.M. (1985) Cloning and sequence analysis of cDNA for human cathepsin D. Proceedings of National Academy of Sciences, USA 82, 4910–4914.Google Scholar
Fujikura, Y. and Karssen, C.M. (1992) Effects of controlled deterioration and osmopriming on protein synthesis of cauliflower seeds during early germination. Seed Science Research 2, 23–31.Google Scholar
Fujikura, Y. and Karssen, C.M. (1994) B. oleracea mRNA for seed imbibition protein. EMBL/Genbank/DDBJ databases, X79330.Google Scholar
Fujikura, Y., Kraak, H.L., Basra, A.S. and Karssen, C.M. (1993) Hydropriming, a simple and inexpensive priming method. Seed Science and Technology 21, 639–642.Google Scholar
Griffin, L.D., MacGregor, G.R., Munzy, D.M., Harter, J., Cook, R.G. and McCabe, E.R.B. (1988) Synthesis of hexokinase I (HKI) cDNA probes by mixed oligonucleotide primed amplification of cDNA (MOPAC) using primer mixtures of high complexity. American Journal of Human Genetics 43, A185.Google Scholar
Heck, G.R., Dorsett, C. and Ho, T.H. (1992) Hordeum vulgare seed imbibition protein (Sip1) gene. EMBL/Genbank/DDBJ databases, M77475.Google Scholar
Lee, P.F., Chow, T.Y., Chen, Z.Y. and Hsing, Y.I.C. (1992) Genomic nucleotide sequence of a soybean seed maturation protein GmPM9 gene. Plant Physiology 100, 2121–2122.Google Scholar
Nagy, F., Kay, S.A. and Chua, N.H. (1988) Analysis of gene expression in transgenic plants. B4:1–29 in Gelvin, S.B., Schilperoort, R.A. and Verma, D.P.S. (Eds) Plant molecular biology manual. Dordrecht, Kluwer Academic Publishers.Google Scholar
Runeberg-Roos, P., Törmäkangas, K. and Östman, A. (1991) Primary structure of a barley-grain aspartic proteinase: A plant aspartic proteinase resembling mammalian cathepsin D. European Journal of Biochemistry 202, 1021–1027.Google Scholar
Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: A laboratories manual. 2nd edition. Cold Spring Harbor, New York, Cold Spring Harbor Laboratories.Google Scholar