Cell biological mechanism for triggering of ABA accumulation under water stress in Vicia faba leaves

Citation
Dp. Zhang et al., Cell biological mechanism for triggering of ABA accumulation under water stress in Vicia faba leaves, SCI CHINA C, 44(4), 2001, pp. 421-428
Citations number
22
Categorie Soggetti
Experimental Biology
Journal title
SCIENCE IN CHINA SERIES C-LIFE SCIENCES
ISSN journal
10069305 → ACNP
Volume
44
Issue
4
Year of publication
2001
Pages
421 - 428
Database
ISI
SICI code
1006-9305(200108)44:4<421:CBMFTO>2.0.ZU;2-Y
Abstract
Water stress-induced ABA accumulation is a cellular signaling process from water stress perception to activation of genes encoding key enzymes of ABA biosynthesis, of which the water stress-signal perception by cells or trigg ering mechanism of the ABA accumulation is the center in the whole process of ABA related-stress signaling in plants. The cell biological mechanism fo r triggering of ABA accumulation under water stress was studied in leaves o f Vicia faba. Mannitol at 890 mmol . kg(-1) osmotic concentration induced a n increase of more than 5 times in ABA concentration in detached leaf tissu es, but the same concentration of mannitol only induced an increase of less than 40 % in ABA concentration in protoplasts. Like in detached leaf tissu es, ABA concentration in isolated cells increased more than 10 times under the treatment of mannitol at 890 mmol . kg(-1) concentration, suggesting th at the interaction between plasmalemma and cell wall was essential to trigg ering of the water stress-induced ABA accumulation. Neither Ca2+-chelating agent EGTA nor Ca2+ channel activator A23187 nor the two cytoskeleton inhib itors, colchicine and cytochalasin B, had any effect on water stress-induce d ABA accumulation. Interestingly water stress-induced ABA accumulation was effectively inhibited by a non-plasmalemma-permeable sulfhydryl-modifier P CMBS (p-chloromercuriphenyl-sulfonic acid), suggesting that plasmalemma pro tein(s) may be involved in the triggering of water stress-induced ABA accum ulation, and the protein may contain sulfhydryl group at its function domai n.