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Photosynthetic Responses of Bermudagrass to Drought Stress Associated with Stomatal and Metabolic Limitations
Author(s) -
Hu Longxing,
Wang Zhaolong,
Huang Bingru
Publication year - 2009
Publication title -
crop science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.76
H-Index - 147
eISSN - 1435-0653
pISSN - 0011-183X
DOI - 10.2135/cropsci2008.12.0697
Subject(s) - rubisco , photosynthesis , cynodon dactylon , biology , stomatal conductance , botany , ecophysiology , photosynthetic capacity , cynodon , horticulture , abscisic acid , agronomy , biochemistry , gene
Plants may survive drought stress by altering photosynthetic metabolism. This study was designed to investigate stomatal and metabolic changes associated with photosynthetic responses to drought for bermudagrass. A hybrid bermudagrass [ Cynodon dactylon (L.) Pers. × C. transvaalensis Burtt Davy, cv. Tifway] and a common bermudagrass ( C. dactylon , cv. C299) were subjected to drought by withholding irrigation in growth chambers. Tifway maintained higher relative water content and lower electrolyte leakage than C299 under drought. Net photosynthetic rate (P n ) and stomatal conductance (g s ) decreased, with more rapid decline in C299, but P n was significantly greater in Tifway than in C299, while g s did not differ between the two genotypes during 14 d of drought. Photochemical efficiency, ribulose‐1,5‐bisphosphate carboxylase:oxygenase (Rubisco) activity, and activation state declined during drought stress, but were higher in Tifway than in C299 within 14 d of treatment. Electrophoretic analysis revealed that at 14 and 18 d of drought, pyruvate orthophosphate dikinase (98 kDa) and Rubisco protein (49 kDa) exhibited severe degradation in C299 but to a lesser extent in Tifway. These results indicated that the superior drought resistance in Tifway could be attributed to higher photosynthetic capacity through the maintenance of higher metabolic activities, as manifested by more active Rubisco enzyme and Rubisco activase and more stable photosynthetic proteins.