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Changes in protein composition in cellular membranes of various parts of secondary dormant cucumber seeds treated with ethanol

Published online by Cambridge University Press:  22 February 2007

Y. Sreenivasulu  and
Dilip Amritphale
Y. Sreenivasulu
Affiliation:
School of Studies in Botany, Vikram University, Ujjain (M.P.) 456 010, India
Dilip Amritphale*
Affiliation:
School of Studies in Botany, Vikram University, Ujjain (M.P.) 456 010, India
*
*Fax: 0091 734 511226, 514550 E-mail: iemps@vsnl.com
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Abstract

Secondary seed dormancy in cucumber (Cucumis sativus L.) cv. Poinsett 76 could be broken with ethanol. Breakage of dormancy was accompanied by significant changes in the composition of membrane proteins in various seed parts. Compared to the intracellular membranes, a change in the protein composition of plasma membranes from the embryonic axis and cotyledons was evident early in the time-course of ethanol-induced germination of dormant seeds. While few alterations in the membrane protein composition in response to ethanol treatment occurred both in dormant and nondormant seeds, a number of changes occurred exclusively in ethanol-treated dormant seeds. Notably, a 14 kD protein in the plasma membrane from the embryonic axis and a 35 kD protein in the microsomal membranes from the perisperm-endosperm envelope disappeared in the ethanol-treated dormant seeds, but not in the ethanol-treated nondormant seeds. Also marked decrease in the content of a 23 kD protein in the plasma membrane from the cotyledons was observed in ethanol-treated dormant seeds only. It is suggested that the particular changes in cellular membrane proteins, which occurred in ethanol-treated dormant seeds much before the first visible indication of germination, might be related to dormancy breaking rather than to the germination process.

Keywords

CucumberCucumis sativus L.ethanolgerminationmembrane proteinsseed dormancy
Type
Research Article
Information
Seed Science Research , Volume 10 , Issue 1 , March 2000 , pp. 61 - 70
Copyright
Copyright © Cambridge University Press 2000

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