Relationship between endosperm cells redox homeostasis and glutenin polymers assembly in developing durum wheat grain
Copyright © 2012 Elsevier Masson SAS. All rights reserved.
| Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 61(2012) vom: 15. Dez., Seite 36-45 |
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| Weitere Verfasser: | , , |
| Format: | Online-Aufsatz |
| Sprache: | English |
| Veröffentlicht: |
2012
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| Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
| Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Antioxidants Plant Proteins Glutens 8002-80-0 Catalase EC 1.11.1.6 Superoxide Dismutase EC 1.15.1.1 mehr... |
| Zusammenfassung: | Copyright © 2012 Elsevier Masson SAS. All rights reserved. Assembly of glutenin polymers was examined for two contrasted durum wheat cultivars in connection with changes in the redox status of the endosperm cells that accompanied grain development. The evolutions of the redox state of ascorbate and glutathione, as well as the activities of antioxidant enzymes were measured. Changes in the size distribution profile and redox state of storage proteins were evaluated, with particular emphasis on protein-bound glutathione (PSSG). At the beginning of grain filling phase, the size distribution profile of proteins included an extra peak shoulder at about 40,000 g mol(-1). The shoulder was assimilated to free glutenin subunits as it disappeared concomitantly with the upturn in glutenin polymers accumulation. Irrespective of cultivars, small SDS-soluble polymers accumulated first, followed by larger and insoluble ones, attesting for a progressive polymerization. During the grain filling phase, catalase (EC 1.11.1.6) activity dropped, reaching a very low level at physiological maturity. During the same period, superoxide dismutase (EC 1.15.1.1) and glutathione reductase (EC 1.6.4.2) activities increased steadily while the equilibrium constant between GSSG and PSSG shifted from 10(-2) to unity. These results demonstrated that grain filling was accompanied by a continuous decrease in cellular redox potential. In this context, formation of protein-bound glutathione would represent a protective mechanism against irreversible thiol oxidation. Storage protein S-glutathionylation instead of limiting glutenin polymer assembly as it has been proposed might be a required intermediate step for glutenin subunits pairing |
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| Beschreibung: | Date Completed 30.05.2013 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
| ISSN: | 1873-2690 |
| DOI: | 10.1016/j.plaphy.2012.08.015 |