Antifreeze protein accumulation in freezing-tolerant cereals

被引:109
作者
Antikainen, M [1 ]
Griffith, M [1 ]
机构
[1] UNIV WATERLOO, DEPT BIOL, WATERLOO, ON N2L 3G1, CANADA
关键词
antifreeze proteins; apoplast; cold acclimation; dicotyledon; freezing tolerance; ice; monocotyledon; pathogenesis-related protein; Poaceae; stress response; PATHOGENESIS-RELATED PROTEINS; THERMAL HYSTERESIS PROTEIN; WINTER RYE LEAVES; CELL-SHAPE; ICE; PLANT; WHEAT; ARABINOXYLANS; BINDING; STRESS;
D O I
10.1034/j.1399-3054.1997.990310.x
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Freezing-tolerant plants withstand extracellular ice formation at subzero temperatures. Previous studies have shown that winter rye (Secale cereale L.) accumulates proteins in the leaf apoplast during cold acclimation that have antifreeze properties and are similar to pathogenesis-related proteins. To determine whether the accumulation of these antifreeze proteins is common among herbaceous plants, we assayed antifreeze activity and total protein content in leaf apoplastic extracts from a number of species grown at low temperature, including both monocotyledons (winter and spring lye, winter and spring wheat, winter barley, spring oats, maize) and dicotyledons (spinach, winter and spring oilseed rape [canola], kale, tobacco). Apoplastic polypeptides were also separated by SDS-PAGE and immunoblotted to determine whether plants generally respond to low temperature by accumulating pathogenesis-related proteins. Our results showed that significant levels of antifreeze activity were present only in the apoplast of freezing-tolerant monocotyledons after cold acclimation at 5/2 degrees C. Moreover, only a closely related group of plants, rye, wheat and barley, accumulated antifreeze proteins similar to pathogenesis-related proteins during cold acclimation. The results indicate that the accumulation of antifreeze proteins is a specific response that may be important in the freezing tolerance of some plants, rather than a general response of all plants to low temperature stress.
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页码:423 / 432
页数:10
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