Changing Ribulose Diphosphate Carboxylase/Oxygenase Activity in Ripening Tomato Fruit

Bravdo, B.; Palgi, Aviva; Lurie, Susan; Frenkél, Chaim

doi:10.1104/pp.60.2.309

Cited by 27 publications

(14 citation statements)

References 15 publications

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“…Ribulose-P2 carboxylase/oxygenase was present in extracts from the outer wall of the pericarp of tomato fruit as observed by other investigators (4,15). The specific activity of ribulose-P2 carboxylase/oxygenase in green tomato fruit was low and declined further with fruit ripening.…”

Section: Discussionsupporting

confidence: 77%

“…Glycolate metabolism, similar to that in leaf peroxisomes (24), has been proposed to be associated with the climacteric respiration in tomatoes (4) and pears (5). On a Chl basis, tomato fruit have substantial ribulose-P22 carboxylase/oxygenase in the outer wall of the pericarp (4,15), and whole fruit flx CO2 by both this enzyme and P-enolpyruvate carboxylase (8). The oxygenase function of ribulose-P2 carboxylase/oxygenase in crude extracts from tomato fruit has been reported to increase relative to carboxylase activity during ripening (4), and glycolate has been observed to accumulate in tomatoes (4) and in strawberries and cherries (13) Ethylene and CO2 evolution were measured by placing fruit in sealed jars equipped with a septum, for I h and taking l-ml air samples with a gas-tight syringe.…”

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confidence: 99%

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Changes in Activity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Three Peroxisomal Enzymes during Tomato Fruit Development and Ripening

Martin¹,

Gauger²,

Tolbert³

1979

Plant Physiol.

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Ribulose-1,5-bisphosphate carboxylase/oxygenase, catalase, glycolate oxidase, and hydroxypyruvate reductase activities on a protein and fresh weight basis were measured over seven stages of tomato fruit development and ripening. Ribulose-1,5-bisphosphate carboxylase decreased steadily during fruit development from 23 ± 8 nmoles per minute per milligram protein at the mature green stage to 13.4 ± 2 at the table ripe stage. There was no change in partially purified preparations of the enzyme in the ratio of carboxylase to oxygenase activity, which was about 10. Catalase activity reached a maximum during the climacteric,.simultaneously with increased ethylene and CO2 formation. Glycolate oxidase activity decreased during early stages of development and was barely detectable at the climacteric. Hydroxypyruvate reductase, associated with serine formation by the glycerate pathway, increased in specific activity during early stages of tomato fruit ripening. In the fruit of the rin tomato mutant, which does not ripen normally, none of these changes in enzyme activity occurred.During the climacteric period of tomato fruit ripening, CO2 evolution and 02 consumption increase 5-to 6-fold (3,10,18 (11), increases in activity in tomato (1), pear (5, 6), and apple (7) during ripening and can be induced by ethylene to increase in activity in preclimacteric mango (20). Glycolate metabolism, similar to that in leaf peroxisomes (24), has been proposed to be associated with the climacteric respiration in tomatoes (4) and pears (5). On a Chl basis, tomato fruit have substantial ribulose-P22 carboxylase/oxygenase in the outer wall of the pericarp (4, 15), and whole fruit flx CO2 by both this enzyme and P-enolpyruvate carboxylase (8). The oxygenase function of ribulose-P2 carboxylase/oxygenase in crude extracts from tomato fruit has been reported to increase relative to carboxylase activity during ripening (4), and glycolate has been observed to accumulate in tomatoes (4) and in strawberries and cherries (13)

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Section: Discussionsupporting

confidence: 77%

mentioning

confidence: 99%

Changes in Activity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Three Peroxisomal Enzymes during Tomato Fruit Development and Ripening

Martin¹,

Gauger²,

Tolbert³

1979

Plant Physiol.

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“…High PEPC activity as well as RuBPC activity was reported in soybean pods (on a fresh weight basis, Hedley et al 1975) and tomato fruits (on a protein basis, Bravd et al 1977). PEPC was more active on a Chl basis in ear parts than in the flag leaves (Singal et al 1986).…”

Section: Differences In O 2 Evolution Rate and Carboxylation Enzymes mentioning

confidence: 93%

Important photosynthetic contribution from the non-foliar green organs in cotton at the late growth stage

Zhang

Luo

et al. 2011

Planta

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Non-foliar green organs are recognized as important carbon sources after leaves. However, the contribution of each organ to total yield has not been comprehensively studied in relation to the time-course of changes in surface area and photosynthetic activity of different organs at different growth stages. We studied the contribution of leaves, main stem, bracts and capsule wall in cotton by measuring their time-course of surface area development, O(2) evolution capacity and photosynthetic enzyme activity. Because of the early senescence of leaves, non-foliar organs increased their surface area up to 38.2% of total at late growth stage. Bracts and capsule wall showed less ontogenetic decrease in O(2) evolution capacity per area and photosynthetic enzyme activity than leaves at the late growth stage. The total capacity for O(2) evolution of stalks and bolls (bracts plus capsule wall) was 12.7 and 23.7% (total ca. 36.4%), respectively, as estimated by multiplying their surface area by their O(2) evolution capacity per area. We also kept the bolls (from 15 days after anthesis) or main stem (at the early full bolling stage) in darkness for comparison with non-darkened controls. Darkening the bolls and main stem reduced the boll weight by 24.1 and 9%, respectively, and the seed weight by 35.9 and 16.3%, respectively. We conclude that non-foliar organs significantly contribute to the yield at the late growth stage.

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“…In the green periearp of wheat grain, a preponderance of labelled products of PEPC such as aspartate, citrate, malate and glutamate have been deteeted after 1-min exposure to "'CO2 in the light (Aoyagi & Bassham, 1984). On a protein basis, reported PEPC : RuBPC ratios for tomato fruit or citrus flower bud are 1.7 to 14 or 4 to 5, respectively (Bravdo et at., 1977;Laval-Martin, Earineau & Diamond, 1977;Vu, Yelenowski & Bausher, 1985), compared with values of O.I for the respective leaf (Vu et al, 1985). In fruit, most of the gaseous CO2 is assimilated from the internal atmosphere where CO2 from mitochondrial respiration accumulates to 1-8% COj in apple or 0.2-3.2% in the pea pod (see section 3).…”

Section: Proposed Rote and Tiinetics Of Pepc In Fruitmentioning

confidence: 99%

Fruit photosynthesis

Blanke

Lenz

1989

Plant Cell & Environment

281

121

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Abstract. In addition to photosynthesis as in the leaf, fruit possess a system which refixes CO2 from the mitochondrial respiration of predominantly imported carbon. This pathway produces malate by the action of phosphoenolpyruvate carboxylase, PEPC, (E.C. 4.1.1.31) and appears to be regulated primarily by the cytosolic concentration of HCO3/CO2 and malate. Malate is stored in the vacuole as malic acid, constituting a major carbon pool and a potential substrate for respiration. The PEPC in apple fruit proves to be an efficient form of the enzyme with low Michaelis constants, i.e. Km = 0.09 mol m‐3 PEP and 0.2 mol m–3 HCO3, and large Ki= 110 mol m‐3 HCO3. In fleshy fruit, chlorophyll and chloroplasts are unevenly distributed; they resemble the C3 sun‐type and arc concentrated in the perivascular tissue, with smaller chloroplasts, fewer grana per chloroplast and a larger degree of vacuolation than commonly found in a leaf of the same species. Fruit photosynthesis often compensates for respiratory CO2 loss in the light. However, due to respiration in the dark, CO2 loss is in excess of photosynthetic gain in the light, such that a continual loss of CO2 was observed in the diurnal cycle and which is maintained throughout fruit development. The rate of CO2 exchange decreases on a fresh weight or surface basis, but increases with fruit ontogeny on a per fruit basis, causing accumulation of several percent CO2 in the internal cavity. Stomata are present in the outer epidermis of those fruits examined, but with a 10‐to 100‐fold lesser frequency than in the abaxial epidermis of leaf of the same species. The number of Stomata is set at anthesis and remained constant, while the stomatal frequency decreases as the fruit surface expands. Stomata are as sensitive as in leaves in the early stages of fruit development, but often are transformed into lenticels during fruit ontogeny, thereby decreasing the permeability of the outer epidermis. The discrepancy between the CO2‐concentrating mechanism provided by PEPC analogous to C4/CAM Photosynthesis and the kinetics of fruit PEPC, characteristic of C3/non‐autotrophic tissue, suggests the definition of a new type of ‘fruit photosynthesis’ rather than its categorization within an existing type.

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Changing Ribulose Diphosphate Carboxylase/Oxygenase Activity in Ripening Tomato Fruit

Cited by 27 publications

References 15 publications

Changes in Activity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Three Peroxisomal Enzymes during Tomato Fruit Development and Ripening

Changes in Activity of Ribulose-1,5-Bisphosphate Carboxylase/Oxygenase and Three Peroxisomal Enzymes during Tomato Fruit Development and Ripening

Important photosynthetic contribution from the non-foliar green organs in cotton at the late growth stage

Fruit photosynthesis

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