Plant Physiology Preview
Published on January 22, 2004; 10.1104/pp.103.030023
Received July 10, 2003
Returned for revision August 22, 2003
Accepted November 6, 2003
Nitric Oxide Functions as a Signal in Salt Resistance in the Calluses from Two Ecotypes of Reed
Liqun Zhao , Feng Zhang , Jinkui Guo , Yingli Yang , Beibei Li , and Lixin Zhang *
State Key Laboratory of Arid Agroecology, School of Life Sciences, Lanzhou University, Lanzhou 730000, People’s Republic of China (L.Z., J.G., B.L., L.Z.); and Environment and Engineering Institute of Cold and Arid Regions, Chinese Academy of Sciences, Lanzhou, 730000, People’s Republic of China (F.Z., Y.Y., L.Z.)
* Corresponding author; email: zhanglixin{at}lzu.edu.cn.
Calluses from two ecotypes of reed (Phragmites communis Trin.) plant (dune reed [DR] and swamp reed [SR]), which show different sensitivity to salinity, were used to study plant adaptations to salt stress. Under 200 mM NaCl treatment, the sodium (Na) percentage decreased, but the calcium percentage and the potassium (K) to Na ratio increased in the DR callus, whereas an opposite changing pattern was observed in the SR callus. Application of sodium nitroprusside (SNP), as a nitric oxide (NO) donor, revealed that NO affected element ratios in both DR and SR calluses in a concentration-dependent manner. N -nitro-L-arginine (an NO synthase inhibitor) and 2-phenyl-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxyde (a specific NO scavenger) counteracted NO effect by increasing the Na percentage, decreasing the calcium percentage and the K to Na ratio. The increased activity of plasma membrane (PM) H+-ATPase caused by NaCl treatment in the DR callus was reversed by treatment with N-nitro-L-arginine and 2-phenyl-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxyde. Western-blot analysis demonstrated that NO stimulated the expression of PM H+-ATPase in both DR and SR calluses. These results indicate that NO serves as a signal in inducing salt resistance by increasing the K to Na ratio, which is dependent on the increased PM H+-ATPase activity.
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