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

Eckardt, Nancy A.; Portis, Archie R.

doi:10.1104/pp.113.1.243

Cited by 79 publications

(49 citation statements)

References 19 publications

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“…Previous studies have shown that purified leaf and recombinant activase are extremely heat-labile if incubated in the absence of ATP (Robinson and Portis, 1989;Holbrook et al, 1991;Eckardt and Portis, 1997). Our results corroborated these findings, because we observed inactivation of both forms upon exposure to relatively moderate temperatures (i.e.…”

Section: Discussionsupporting

confidence: 82%

The Two Forms of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Differ in Sensitivity to Elevated Temperature

1997

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Ribulose-l,5-bisphosphate carboxylase/oxygenase activase often consists of two polypeptides that arise from alternative splicing of pre-mRNA. I n this study recombinant versions of the spinach (Spinacea oleracea L.) 45-and 41-kD forms of activase were analyzed for their response to temperature. The temperature optimum for ATP hydrolysis by the 45-kD form was 45"C, approximately 13°C higher than the 41 -kD form. When the two forms were mixed, the temperature response of the hybrid enzyme was similar to the 45-kD form. I n the absence of adenine nucleotide, preincubation of either activase form at temperatures above 25°C inactivated ATPase activity. Adenosine 5'-(y-thio)triphosphate, but not ADP, significantly enhanced the thermostability of the 45-kD form but was much less effective for the 41-kD form. lntrinsic fluorescence showed that the adenosine 5'-(y-thio)triphosphate-induced subunit aggregation was lost at a much lower temperature for the 41-kD than for the 45-kD form. However, the two activase forms were equally susceptible to limited proteolysis after heat treatment. The results indicate that (a) the 45-kD form is more thermostable than, and confers increased thermal stability to, the 41 -kD form, and (b) a loss of subunit interactions, rather than enzyme denaturation, appears to be the initial cause of temperature inactivation of activase.Zielinski, 1991a). In spinach the 45-and 41-kD activase polypeptides are identical except for 37 additional amino acids on the C-terminal end of the 45-kD form. Both the 45-and the 41-kD forms of spinach activase catalyze ATP hydrolysis, as well as activate Rubisco (Shen et al., 1991). However, aside from relatively minor differences in ATP binding (Shen et al., 1991), there is no information about other functional differences between the two forms of activase.In this paper we report the effect of elevated temperature on the 45-and 41-kD forms of recombinant spinach activase. Our results show that the two forms differ significantly in thermal stability and, when mixed, the thermal stability of the hybrid enzyme is similar to the 45-kD form. The greater thermal stability of the 45-kD form appears to be related to tighter subunit association. MATERIALS AND METHODSCloning and lsolation of the Long a n d Short Forms of Rubisco ActivaseClones encoding the 45-and 41-kD forms of spinach (Spinacea oleracea L.) Rubisco activase (pPLEX1.9 and Rubisco activase is a chloroplastic enzyme that regulates pPLEX1.6), described by Werneke et al. (1989) and Shen et the activity of Rubisco in a light-dependent manner (Salal. (1991) Salvucci and Ogren, 1996). Once freed of these plasmids were used for expression of recombinant activase compounds, Rubisco can be activated by spontaneous car- (van de Loo and Salvucci, 1996). Recombinant Rubisco bamylation with CO, (Lorimer and Miziorko, 1980). activase was purified from the cells, as described by SalIn most of the plant species that have been examined, vucci and Klein (1994), with the modifications noted by van Rubisco activase is composed...

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Section: Discussionsupporting

confidence: 82%

The Two Forms of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Differ in Sensitivity to Elevated Temperature

1997

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“…Thus, our results seem to indicate that the accumulation of GB in vivo leads to increased thermotolerance of Rubisco activase. This function of GB is of significance for increasing tolerance of plants to high temperatures since Rubisco activase has been shown to be particularly sensitive to inactivation by high temperatures (Crafts-Brandner et al, 1997;Eckhardt and Portis, 1997).…”

Section: Discussionmentioning

confidence: 99%

Genetic Engineering of the Biosynthesis of Glycinebetaine Enhances Photosynthesis against High Temperature Stress in Transgenic Tobacco Plants

2005

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Genetically engineered tobacco (Nicotiana tabacum) with the ability to synthesis glycinebetaine was established by introducing the BADH gene for betaine aldehyde dehydrogenase from spinach (Spinacia oleracea). The genetic engineering enabled the plants to accumulate glycinebetaine mainly in chloroplasts and resulted in enhanced tolerance to high temperature stress during growth of young seedlings. Moreover, CO 2 assimilation of transgenic plants was significantly more tolerant to high temperatures than that of wild-type plants. The analyses of chlorophyll fluorescence and the activation of Rubisco indicated that the enhancement of photosynthesis to high temperatures was not related to the function of photosystem II but to the Rubisco activase-mediated activation of Rubisco. Western-blotting analyses showed that high temperature stress led to the association of Rubisco activase with the thylakoid membranes from the stroma fractions. However, such an association was much more pronounced in wild-type plants than in transgenic plants. The results in this study suggest that under high temperature stress, glycinebetaine maintains the activation of Rubisco by preventing the sequestration of Rubisco activase to the thylakoid membranes from the soluble stroma fractions and thus enhances the tolerance of CO 2 assimilation to high temperature stress. The results seem to suggest that engineering of the biosynthesis of glycinebetaine by transformation with the BADH gene might be an effective method for enhancing high temperature tolerance of plants.High temperature stress is one of the environmental factors that limit plant growth (Levitt, 1980;Boyer, 1982;Frova, 1997). Photosynthesis is one of the physiological processes that are most sensitive to high temperature stress (Berry and Bjö rkman, 1980). Inhibition of photosynthesis by high temperature stress is a common occurrence for plants in tropical and subtropical regions and the temperate zones where plants are exposed periodically to high temperatures (Larcher, 1995). It is well documented that high temperature stress causes damage to photosynthetic electron transport (Berry and Björkman, 1980). For many years, PSII has long been considered the most heatsensitive component of the photosynthetic apparatus (Berry and Bjö rkman, 1980). However, it appears that PSII is unaffected at temperatures that inhibit CO 2 fixation (Weis, 1981a(Weis, , 1981b, and that PSII is only inhibited by severe heat stress when the temperature is higher than 45°C (Havaux, 1993(Havaux, , 1996. Recent studies seem to support that PSII activity is not limiting at temperatures that inhibit CO 2 fixation and that CO 2 fixation is most sensitive to heat stress due to the inhibition of activation of Rubisco via a direct effect on Rubisco activase (Feller et al., 1998; Crafts-Brandner, 2004a, 2004b;Haldimann and Feller, 2004).Glycinebetaine (GB) is one of the organic compatible solutes that can accumulate rapidly in many plants under salinity stress, drought, and low temperature (McCue and Hanson, 1990...

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“…Heat stress primarily affects thermolabile components, especially photosystem II (PSII) [1] [2] [5]- [7] and Rubisco activase in the Calvin cycle [8]- [10]. Physiological and photosynthetic functions could thus be significantly impaired by elevated heat stress.…”

Section: Introductionmentioning

confidence: 99%

Physiological Performances of Temperate Vegetables with Response to Chronic and Acute Heat Stress

Lai¹,

He²

2016

AJPS

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In face of climate change catastrophes, understanding the thermal limits and optimal physiological thermal window food crop is of particular urgency. This research aims to evaluate: 1) how physiological performances of plant will change with increasing chronic and acute heat stress; 2) if the examined parameters form a hierarchy in terms of thermal tolerance; and 3) the optimal thermal window and critical temperatures of the examined plants with response to chronic and acute heat stress. Six temperate vegetables were subjected to chronic and acute heat stress and a suite of physiological parameters were evaluated. Dose responses were observed in shoot fresh weight, photosynthetic gas exchange, photosynthetic oxygen evolution, electron transfer rate, photo-and non-photochemical quenching with significant drop in performance as early as 28˚C for selected species. Conversely, ratio of variable to maximum fluorescence (F v /F m ) was not affected by heat stress until 46˚C in chronic heat stress. Examining the temperature at which a measured parameter's performance dropped by 50% compared to control (LT 50 ), a distinct hierarchy of the indices was observed for Canasta, recombinant inbred line 141, Lactuca serriola and Lactuca sativa (L. "Salinas"): shoot fresh weight, representing the highest integrated level of photosynthesis was the most sensitive to thermal stress (28˚C -30˚C), followed by oxygen evolution (35˚C -45˚C) while non-photochemical and photochemical quenching which is subcellular function of stress alleviation had a much higher capacity failure temperature (47˚C -60˚C). It is expected that F v /F m ratio, a measurement of sub-cellular structural integrity, will approach that of non-photochemical and photochemical quenching, if not exceeding it. By examining the photosynthetic parameters via their hierarchy of biological organization, it can be inferred that plants like Arugula and recombinant inbred line 192 are already operating near their thermal limit and have less energetic investment into heat stress mediation whereas L. serriola prioritizes thermal tolerance at the expense of photosynthesis efficiency.

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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

Cited by 79 publications

References 19 publications

The Two Forms of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Differ in Sensitivity to Elevated Temperature

The Two Forms of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase Activase Differ in Sensitivity to Elevated Temperature

Genetic Engineering of the Biosynthesis of Glycinebetaine Enhances Photosynthesis against High Temperature Stress in Transgenic Tobacco Plants

Physiological Performances of Temperate Vegetables with Response to Chronic and Acute Heat Stress

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