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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.

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