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

Crafts‐Brandner, Steven J.; Law, R. David

doi:10.1007/s004250000364

Cited by 158 publications

(101 citation statements)

References 25 publications

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“…For example, malate inhibited PEP carboxylase activity by about 50% when leaf temperature was 28°C, whereas this inhibition was 59% and 66% when leaf temperature was 40°C and 45°C, respectively. Similar to the two C4 enzymes, and consistent with results for C3 plant species (Weis, 1981a(Weis, , 1981bCrafts-Brandner and Law, 2000), the total activity of Rubisco was not affected by leaf temperatures up to at least 45°C (Table I). However, the activation state of Rubisco was decreased progressively as leaf temperature was increased above 28°C (Fig.…”

Section: Resultssupporting

confidence: 72%

Sensitivity of Photosynthesis in a C4 Plant, Maize, to Heat Stress

2002

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Our objective was to determine the sensitivity of components of the photosynthetic apparatus of maize (Zea mays), a C4 plant, to high temperature stress. Net photosynthesis (Pn) was inhibited at leaf temperatures above 38°C, and the inhibition was much more severe when the temperature was increased rapidly rather than gradually. Transpiration rate increased progressively with leaf temperature, indicating that inhibition was not associated with stomatal closure. Nonphotochemical fluorescence quenching (qN) increased at leaf temperatures above 30°C, indicating increased thylakoid energization even at temperatures that did not inhibit Pn. Compared with CO 2 assimilation, the maximum quantum yield of photosystem II (F v /F m ) was relatively insensitive to leaf temperatures up to 45°C. The activation state of phosphoenolpyruvate carboxylase decreased marginally at leaf temperatures above 40°C, and the activity of pyruvate phosphate dikinase was insensitive to temperature up to 45°C. The activation state of Rubisco decreased at temperatures exceeding 32.5°C, with nearly complete inactivation at 45°C. Levels of 3-phosphoglyceric acid and ribulose-1,5-bisphosphate decreased and increased, respectively, as leaf temperature increased, consistent with the decrease in Rubisco activation. When leaf temperature was increased gradually, Rubisco activation acclimated in a similar manner as Pn, and acclimation was associated with the expression of a new activase polypeptide. Rates of Pn calculated solely from the kinetics of Rubisco were remarkably similar to measured rates if the calculation included adjustment for temperature effects on Rubisco activation. We conclude that inactivation of Rubisco was the primary constraint on the rate of Pn of maize leaves as leaf temperature increased above 30°C.It has long been recognized that C4 plant species have a higher temperature optimum for photosynthesis than C3 plants due to the operation of a CO 2 -concentrating system that inhibits Rubisco oxygenase activity (Berry and Bjö rkman, 1980;Edwards and Walker, 1983). In C3 plants, inhibition of net photosynthesis (Pn) at moderately high temperatures has usually been ascribed to an increase in the ratio of Rubisco oxygenase:Rubisco carboxylase activities. As temperature increases, the ratio of dissolved O 2 /CO 2 and the specificity of Rubisco for O 2 increase, thus favoring oxygenase activity (Monson et al., 1982; Jordan and Ogren, 1984; Sage and Sharkey, 1987) and resulting in inhibition of Pn. As a consequence, when C3 plants are exposed to high CO 2 and/or low O 2 , i.e. conditions that reduce oxygenase activity, the temperature optimum for Pn is increased (Berry and Bjö rkman, 1980;Edwards and Walker, 1983).For C3 and C4 plants, the temperature range for optimum Pn is broad, and at temperatures above this range, Pn decreases (Edwards and Walker, 1983). Temperature-induced decreases in Pn in C3 species are closely associated with inactivation of Rubisco (Law and Crafts-Brandner, 1999), and when the activation state of Rubisco and g...

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Section: Resultssupporting

confidence: 72%

Sensitivity of Photosynthesis in a C4 Plant, Maize, to Heat Stress

2002

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“…High temperature result in the decreased solubility of O 2 and CO 2 however, increased photorespiration and lower photosynthesis is the result of increased level of CO 2 than O 2 [71]. In addition, decreased activity of Rubisco at high temperature is primarily due to inhibition of the enzyme Rubisco activase which becomes unable to overcome the inherently faster rates of Rubisco inactivation [72][73][74]. Amongst the photosynthetic apparatus photosystem II being more tolerant to drought stress than heat relatively plays a key role in leaf photosynthesis [75].…”

Section: Effects Of Heat Stress On Plant Physiologymentioning

confidence: 99%

Impacts of Heat Stress on Wheat: A Critical Review

Iqbal¹,

Raja²,

Yasmeen³

et al. 2017

Adv Crop Sci Tech

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A brief review is given of investigations on stress-induced alterations in the yield of different biochemical contents in wheat. Wheat is major cereal crop for fulfilling the calories demands of growing population. Alterations in the worldwide climate are predicted to have critical sentence for crop production. Abiotic stresses such as heat and drought are major abiotic stresses restraining crop production. Heat stress reduces wheat growth by upsetting various physiological and biochemical processes and the developmental stage of the plant is critical in demonstrating the vulnerability of various species and cultivars subjected to high temperature. Heat stress did not affect the protein content but there is strong correlation between leaf nitrogen content and grain protein content. Induction of HSPs seems to be the universal response and adaptation to temperature stress. The synthesis of HSPs is believed to play significant role either in preventing or minimizing the adverse effects of high temperature both at molecular and cellular levels. Wheat has the tendency to adopt diverse types of responses to temperature stress as well as a heat shock by developing thermo-tolerance for the enhancement of the grain quality and yield.

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“…It has been proposed that Rubisco activation state decreases at high temperature, because the activity of Rubisco activase is insufficient to keep pace with the faster rates of Rubisco inactivation at high temperatures (Crafts-Brandner and Salvucci, 2000;Crafts-Brandner, 2004a, 2004c;Kim and Portis, 2006). In in vitro assays using purified Rubisco and Rubisco activase, the activity of Rubisco activase was sufficient for the activation of Rubisco at the optimum temperature but not at high temperatures (Crafts-Brandner and Salvucci, 2000;Crafts-Brandner, 2004a, 2004c (Crafts-Brandner and Law, 2000;Salvucci and Crafts-Brandner, 2004b). Moreover, the rates of inhibitor formation by misprotonation of RuBP during catalysis increased at higher temperatures (Salvucci and Crafts-Brandner, 2004c;Kim and Portis, 2006).…”

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confidence: 99%

Effect of Rubisco Activase Deficiency on the Temperature Response of CO2 Assimilation Rate and Rubisco Activation State: Insights from Transgenic Tobacco with Reduced Amounts of Rubisco Activase

Yamori

Caemmerer

2009

Plant Physiology

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The activation of Rubisco in vivo requires the presence of the regulatory protein Rubisco activase. To elucidate its role in maintaining CO 2 assimilation rate at high temperature, we examined the temperature response of CO 2 assimilation rate at 380 mL L 21 CO 2 concentration (A 380 ) and Rubisco activation state in wild-type and transgenic tobacco (Nicotiana tabacum) with reduced Rubisco activase content grown at either 20°C or 30°C. Analyses of gas exchange and chlorophyll fluorescence showed that in the wild type, A 380 was limited by ribulose 1,5-bisphosphate regeneration at lower temperatures, whereas at higher temperatures, A 380 was limited by ribulose 1,5-bisphosphate carboxylation irrespective of growth temperatures. Growth temperature induced modest differences in Rubisco activation state that declined with measuring temperature, from mean values of 76% at 15°C to 63% at 40°C in wild-type plants. At measuring temperatures of 25°C and below, an 80% reduction in Rubisco activase content was required before Rubisco activation state was decreased. Above 35°C, Rubisco activation state decreased slightly with more modest decreases in Rubisco activase content, but the extent of the reductions in Rubisco activation state were small, such that a 55% reduction in Rubisco activase content did not alter the temperature sensitivity of Rubisco activation and had no effect on in vivo catalytic turnover rates of Rubisco. There was a strong correlation between Rubisco activase content and Rubisco activation state once Rubisco activase content was less that 20% of wild type at all measuring temperatures. We conclude that reduction in Rubisco activase content does not lead to an increase in the temperature sensitivity of Rubisco activation state in tobacco.

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

Cited by 158 publications

References 25 publications

Sensitivity of Photosynthesis in a C4 Plant, Maize, to Heat Stress

Sensitivity of Photosynthesis in a C4 Plant, Maize, to Heat Stress

Impacts of Heat Stress on Wheat: A Critical Review

Effect of Rubisco Activase Deficiency on the Temperature Response of CO2 Assimilation Rate and Rubisco Activation State: Insights from Transgenic Tobacco with Reduced Amounts of Rubisco Activase

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