Effect of heat stress on the inhibition and recovery of the ribulose-1,5-bisphosphate carboxylase/oxygenase activation state

被引:137
作者
Crafts-Brandner, SJ [1 ]
Law, RD [1 ]
机构
[1] USDA ARS, Western Cotton Res Lab, Phoenix, AZ 85040 USA
关键词
Gossypium (heat stress; Rubisco); heat stress; photosynthesis; ribulose-1,5-bisphosphate carboxylase/oxygenase; Rubisco activase;
D O I
10.1007/s004250000364
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
Experiments were conducted to determine the relative contributions of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco; EC 4.1.1.39) activation state vis-g-vis Rubisco activase and metabolite levels to the inhibition of cotton (Gossypium hirsutum L.) photosynthesis by heat stress. Exposure of leaf tissue in the light to temperatures of 40 or 45 degreesC decreased the activation state of Rubisco to levels that were 65 or 10%, respectively, of the 28 degreesC control. Ribulose-1,5-bisphosphate (RuBP) levels increased in heat-stressed leaves, whereas the 3-phosphoglyceric acid pool was depleted. Heat stress did not affect Rubisco per se, as full activity could be restored by incubation with CO2 and Mg2+. Inhibition and recovery of Rubisco activation state and carbon dioxide exchange rate (CER) were closely related under moderate heat stress (up to 42.5 degreesC). Moderate heat stress had negligible effect on Fv/Fm, the maximal quantum yield of photosystem II. In contrast, severe heat stress (45 degreesC) caused significant and irreversible damage to Rubisco activation, CER, and Fv/Fm. The rate of Rubisco activation after alleviating moderate beat stress was comparable to that of controls, indicating rapid reversibility of the process. However, moderate heat stress decreased both the rate and final extent of CER activation during dark-to-light transition. Treatment of cotton leaves with methyl viologen or an oxygen-enriched atmosphere reduced the effect of heat stress on Rubisco inactivation. Both treatments also reduced tissue RuBP levels, indicating that the amount of RuBP present during heat stress may influence the degree of Rubisco inactivation. Under both photorespiratory and non-photorespiratory conditions, the inhibition of the CER during heat stress could be completely reversed by increasing the internal partial pressure of CO2 (Ci). However, the inhibition of the CER by nigericin, a K+ ionophore, was not reversible when the Ci was increased at ambient or high temperature. Our results indicate that inhibition of photosynthesis by moderate heat stress is not caused by inhibition of the capacity for RuBP regeneration. We conclude that heat stress inhibits Rubisco activation via a rapid and direct effect on Rubisco activase, possibly by perturbing Rubisco activase subunit interactions with each other or with Rubisco.
引用
收藏
页码:67 / 74
页数:8
相关论文
共 32 条
[1]  
[Anonymous], 1987, Plant Response to Stress
[2]   PHOTOSYNTHETIC RESPONSE AND ADAPTATION TO TEMPERATURE IN HIGHER-PLANTS [J].
BERRY, J ;
BJORKMAN, O .
ANNUAL REVIEW OF PLANT PHYSIOLOGY AND PLANT MOLECULAR BIOLOGY, 1980, 31 :491-543
[3]   PROTEIN-BOUND RIBULOSE BISPHOSPHATE CORRELATES WITH DEACTIVATION OF RIBULOSE BISPHOSPHATE CARBOXYLASE IN LEAVES [J].
BROOKS, A ;
PORTIS, AR .
PLANT PHYSIOLOGY, 1988, 87 (01) :244-249
[4]   Heat sensitivity of chloroplasts and leaves: Leakage of protons from thylakoids and reversible activation of cyclic electron transport [J].
Bukhov, NG ;
Wiese, C ;
Neimanis, S ;
Heber, U .
PHOTOSYNTHESIS RESEARCH, 1999, 59 (01) :81-93
[5]   REGULATION OF RIBULOSE 1,5-DIPHOSPHATE CARBOXYLASE BY SUBSTRATES AND OTHER METABOLITES - FURTHER EVIDENCE FOR SEVERAL TYPES OF BINDING-SITES [J].
CHU, DK ;
BASSHAM, JA .
PLANT PHYSIOLOGY, 1975, 55 (04) :720-726
[6]   The two forms of ribulose-1,5-bisphosphate carboxylase/oxygenase activase differ in sensitivity to elevated temperature [J].
CraftsBrandner, SJ ;
vandeLoo, FJ ;
Salvucci, ME .
PLANT PHYSIOLOGY, 1997, 114 (02) :439-444
[7]   Heat denaturation profiles of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and rubisco activase and the inability of Rubisco activase to restore activity of heat-denatured Rubisco [J].
Eckardt, NA ;
Portis, AR .
PLANT PHYSIOLOGY, 1997, 113 (01) :243-248
[8]   A BIOCHEMICAL-MODEL OF PHOTOSYNTHETIC CO2 ASSIMILATION IN LEAVES OF C-3 SPECIES [J].
FARQUHAR, GD ;
CAEMMERER, SV ;
BERRY, JA .
PLANTA, 1980, 149 (01) :78-90
[9]   Moderately high temperatures inhibit ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) activase-mediated activation of Rubisco [J].
Feller, U ;
Crafts-Brandner, SJ ;
Salvucci, ME .
PLANT PHYSIOLOGY, 1998, 116 (02) :539-546
[10]   Regulation of Rubisco activation in antisense plants of tobacco containing reduced levels of Rubisco activase [J].
Hammond, ET ;
Andrews, TJ ;
Mott, KA ;
Woodrow, IE .
PLANT JOURNAL, 1998, 14 (01) :101-110