Glutamine synthetase and glutamate dehydrogenase contribute differentially to proline accumulation in leaves of wheat (Triticum aestivum) seedlings exposed to different salinity

被引:130
作者
Wang, Zhi-Qiang [1 ]
Yuan, Yong-Ze [1 ]
Ou, Ji-Quan [1 ]
Lin, Qing-Hua [1 ]
Zhang, Chu-Fu [1 ]
机构
[1] Wuhan Univ, Coll Life Sci, Key Lab MOE Plant Dev Biol, Wuhan 430072, Peoples R China
基金
中国国家自然科学基金;
关键词
glutamate dehydrogenase; glutamine synthetase; proline; salinity; wheat;
D O I
10.1016/j.jplph.2006.05.001
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
To investigate the roles of ammonium-assimilating enzymes in proline synthesis under salinity stress, the activities of glutamine synthetase (GS; EC 6.3.1.2) and NADH-dependent glutamate dehydrogenase (NADH-GDH; EC 1.4.1.2) were determined in leaves of wheat (Triticum aestivum) seedlings exposed to salt stress at 150 and 300 mM NaCl for 5 d. At the lower salinity, only GS activity increased markedly. At 300 mM NaCl, however, NADH-GDH activity increased while GS activity decreased. A significant accumulation of proline was found only at high-salinity exposure while glutamate, a proline precursor, increased dramatically under both low and high salinity. These data suggests that GS-catalysis might be the main glutamate synthesis pathway under low salinity. At 300 mM NaCl, glutamate seems to be preferentially produced through the process catalyzed by NADH-GDH. The increase of ammonium in salinity-stressed wheat seedlings might have resulted from increased photorespiration, which is responsible for the higher NADH-GDH activity. The activity of Delta(1)-pyrroline-5-carboxylate reductase (P5CR; EC 1.5.1.2) was significantly enhanced at 300 mM NaCl but remained unchanged at 150 mM. Delta(1)-Pyrroline-5-carboxylate synthetase (P5CS) activity did not show a specific response, indicating that P5CR might be the limiting step in proline synthesis from glutamate at high salinity. (c) 2006 Elsevier GmbH. All rights reserved.
引用
收藏
页码:695 / 701
页数:7
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