1. AMINOPEPTIDASE ACTIVITIES IN ROOTS AND LEAVES OF DROUGHT STRESSED WINTER WHEAT SEEDLINGS.
- Author
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Simova-Stoilova, L., Kirova, E., Zehirov, G., Vaseva, I., and Feller, U.
- Subjects
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AMINOPEPTIDASES , *WINTER wheat , *PLANT root physiology - Abstract
In order to evaluate the role of aminopeptidases (APs) in drought response and their potential as protein markers to distinguish between stress tolerant and sensitive varieties, various AP activities were studied in roots and leaves of winter wheat seedlings, subjected to severe but recoverable soil drought stress. Two varieties with contrasting drought tolerance - Yantar (drought tolerant) and Miziya (sensitive) were compared. Activity changes under severe water stress and subsequent recovery were related to changes in the pools of the major redox buffers ascorbate and glutathione, changes in protein profiles and total proteolysis in roots and leaves. Glutathione was responsive to drought both in roots and leaves, with increased total pool and transient rise in the oxidized form; stronger response in the roots of Yantar was observed. The sensitive variety had higher ascorbate content in leaves under stress. Severe drought led to reversible changes in protein profiles and increase in major protease bands in leaves but not in roots. AP activities were partly independent from the predominant endoprotease activities. Highest activities in roots were detected with substrates releasing terminal leucine, lysine and metionine. In stressed leaves AP activities toward most of the substrates increased under drought, without clear differences comparing varieties. Activities tested with Gly-pNA were raised in leaves only in recovery from stress. In roots, the tolerant variety Yantar presented increased AP activities under stress with most of the substrates used except Leu-pNA and Phe-pNA, whereas the sensitive variety Miziya had almost unchanged AP activities. Based on activity profile changes, at least two different AP enzymes should exist in wheat. It remains to be established which activities towards different substrates reflect distinct aminopeptidases. [ABSTRACT FROM AUTHOR]
- Published
- 2016